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UniProtKB - P0ACC7 (GLMU_ECOLI)
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>sp|P0ACC7|GLMU_ECOLI Bifunctional protein GlmU OS=Escherichia coli (strain K12) OX=83333 GN=glmU PE=1 SV=1 MLNNAMSVVILAAGKGTRMYSDLPKVLHTLAGKAMVQHVIDAANELGAAHVHLVYGHGGD LLKQALKDDNLNWVLQAEQLGTGHAMQQAAPFFADDEDILMLYGDVPLISVETLQRLRDA KPQGGIGLLTVKLDDPTGYGRITRENGKVTGIVEHKDATDEQRQIQEINTGILIANGADM KRWLAKLTNNNAQGEYYITDIIALAYQEGREIVAVHPQRLSEVEGVNNRLQLSRLERVYQ SEQAEKLLLAGVMLRDPARFDLRGTLTHGRDVEIDTNVIIEGNVTLGHRVKIGTGCVIKN SVIGDDCEISPYTVVEDANLAAACTIGPFARLRPGAELLEGAHVGNFVEMKKARLGKGSK AGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTIIGDDVFVGSDTQLVAPVTVGKGAT IAAGTTVTRNVGENALAISRVPQTQKEGWRRPVKKKCommunity curation ()Add a publicationFeedback
Protein
Bifunctional protein GlmU
Gene
glmU
Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
UniRule annotation<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
5 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.9"Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily."
Brown K., Pompeo F., Dixon S., Mengin-Lecreulx D., Cambillau C., Bourne Y.
EMBO J. 18:4096-4107(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF THE TRUNCATED FORM AND IN COMPLEX WITH UDP-GLCNAC, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-14; ARG-18 AND LYS-25, SUBCELLULAR LOCATION, SUBUNIT. - Ref.12"In vitro validation of acetyltransferase activity of GlmU as an antibacterial target in Haemophilus influenzae."
Buurman E.T., Andrews B., Gao N., Hu J., Keating T.A., Lahiri S., Otterbein L.R., Patten A.D., Stokes S.S., Shapiro A.B.
J. Biol. Chem. 286:40734-40742(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 233-452 ACETYL-COA ANALOG, FUNCTION, ACTIVITY REGULATION, SUBUNIT. - Ref.13"Inhibitors of acetyltransferase domain of N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU). Part 1: Hit to lead evaluation of a novel arylsulfonamide series."
Green O.M., McKenzie A.R., Shapiro A.B., Otterbein L., Ni H., Patten A., Stokes S., Albert R., Kawatkar S., Breed J.
Bioorg. Med. Chem. Lett. 22:1510-1519(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 227-456, FUNCTION, ACTIVITY REGULATION, SUBUNIT.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- acetyl-CoAEC:2.3.1.157
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Manual assertion according to rulesi
3 PublicationsManual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.9"Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily."
Brown K., Pompeo F., Dixon S., Mengin-Lecreulx D., Cambillau C., Bourne Y.
EMBO J. 18:4096-4107(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF THE TRUNCATED FORM AND IN COMPLEX WITH UDP-GLCNAC, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-14; ARG-18 AND LYS-25, SUBCELLULAR LOCATION, SUBUNIT.
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Manual assertion according to rulesi
3 PublicationsManual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.9"Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily."
Brown K., Pompeo F., Dixon S., Mengin-Lecreulx D., Cambillau C., Bourne Y.
EMBO J. 18:4096-4107(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF THE TRUNCATED FORM AND IN COMPLEX WITH UDP-GLCNAC, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-14; ARG-18 AND LYS-25, SUBCELLULAR LOCATION, SUBUNIT.
Source: Rhea- Search for this reaction in UniProtKB.
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acetyl-CoA- Search proteins in UniProtKB for this molecule.
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+α-D-glucosamine 1-phosphate- Search proteins in UniProtKB for this molecule.
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=CoA- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+N-acetyl-α-D-glucosamine 1-phosphate- Search proteins in UniProtKB for this molecule.
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- H+EC:2.7.7.23
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Manual assertion according to rulesi
3 PublicationsManual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.9"Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily."
Brown K., Pompeo F., Dixon S., Mengin-Lecreulx D., Cambillau C., Bourne Y.
EMBO J. 18:4096-4107(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF THE TRUNCATED FORM AND IN COMPLEX WITH UDP-GLCNAC, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-14; ARG-18 AND LYS-25, SUBCELLULAR LOCATION, SUBUNIT.
- Search proteins in UniProtKB for this EC number.
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Manual assertion according to rulesi
3 PublicationsManual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.9"Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily."
Brown K., Pompeo F., Dixon S., Mengin-Lecreulx D., Cambillau C., Bourne Y.
EMBO J. 18:4096-4107(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF THE TRUNCATED FORM AND IN COMPLEX WITH UDP-GLCNAC, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-14; ARG-18 AND LYS-25, SUBCELLULAR LOCATION, SUBUNIT.
Source: Rhea- Search for this reaction in UniProtKB.
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H+- Search proteins in UniProtKB for this molecule.
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+N-acetyl-α-D-glucosamine 1-phosphate- Search proteins in UniProtKB for this molecule.
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=diphosphate- Search proteins in UniProtKB for this molecule.
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+UDP-N-acetyl-α-D-glucosamine- Search proteins in UniProtKB for this molecule.
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<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Mg2+
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Manual assertion based on experiment ini
- Ref.11"Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products."
Olsen L.R., Vetting M.W., Roderick S.L.
Protein Sci. 16:1230-1235(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC, COA AND MAGNESIUM IONS, COFACTOR, SUBUNIT.
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Manual assertion based on experiment ini
- Ref.10"Structure of the Escherichia coli glmU pyrophosphorylase and acetyltransferase active sites."
Olsen L.R., Roderick S.L.
Biochemistry 40:1913-1921(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC; COA AND COBALT ION, COFACTOR, SUBUNIT.
Manual assertion based on experiment ini
- Ref.10"Structure of the Escherichia coli glmU pyrophosphorylase and acetyltransferase active sites."
Olsen L.R., Roderick S.L.
Biochemistry 40:1913-1921(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC; COA AND COBALT ION, COFACTOR, SUBUNIT. - Ref.11"Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products."
Olsen L.R., Vetting M.W., Roderick S.L.
Protein Sci. 16:1230-1235(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC, COA AND MAGNESIUM IONS, COFACTOR, SUBUNIT.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Inhibited by its reaction product N-acetylglucosamine-1-phosphate and by UDP-N-acetylmuramic acid, which is one of the first precursors specific for the peptidoglycan pathway.3 Publications
Manual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.12"In vitro validation of acetyltransferase activity of GlmU as an antibacterial target in Haemophilus influenzae."
Buurman E.T., Andrews B., Gao N., Hu J., Keating T.A., Lahiri S., Otterbein L.R., Patten A.D., Stokes S.S., Shapiro A.B.
J. Biol. Chem. 286:40734-40742(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 233-452 ACETYL-COA ANALOG, FUNCTION, ACTIVITY REGULATION, SUBUNIT. - Ref.13"Inhibitors of acetyltransferase domain of N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU). Part 1: Hit to lead evaluation of a novel arylsulfonamide series."
Green O.M., McKenzie A.R., Shapiro A.B., Otterbein L., Ni H., Patten A., Stokes S., Albert R., Kawatkar S., Breed J.
Bioorg. Med. Chem. Lett. 22:1510-1519(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 227-456, FUNCTION, ACTIVITY REGULATION, SUBUNIT.
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=0.018 mM for N-acetylglucosamine 1-phosphate3 Publications
Manual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional protein glmU from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes."
Pompeo F., van Heijenoort J., Mengin-Lecreulx D.
J. Bacteriol. 180:4799-4803(1998) [PubMed] [Europe PMC] [Abstract]Cited for: MUTAGENESIS OF CYS-296; CYS-307; CYS-324 AND CYS-385, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=0.07 mM for alpha-D-glucosamine 1-phosphate1 Publication
Manual assertion based on experiment ini
- Ref.9"Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily."
Brown K., Pompeo F., Dixon S., Mengin-Lecreulx D., Cambillau C., Bourne Y.
EMBO J. 18:4096-4107(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF THE TRUNCATED FORM AND IN COMPLEX WITH UDP-GLCNAC, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-14; ARG-18 AND LYS-25, SUBCELLULAR LOCATION, SUBUNIT.
- KM=0.1 mM for UTP1 Publication
Manual assertion based on experiment ini
- Ref.9"Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily."
Brown K., Pompeo F., Dixon S., Mengin-Lecreulx D., Cambillau C., Bourne Y.
EMBO J. 18:4096-4107(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF THE TRUNCATED FORM AND IN COMPLEX WITH UDP-GLCNAC, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-14; ARG-18 AND LYS-25, SUBCELLULAR LOCATION, SUBUNIT.
- KM=0.15 mM for alpha-D-glucosamine 1-phosphate3 Publications
Manual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional protein glmU from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes."
Pompeo F., van Heijenoort J., Mengin-Lecreulx D.
J. Bacteriol. 180:4799-4803(1998) [PubMed] [Europe PMC] [Abstract]Cited for: MUTAGENESIS OF CYS-296; CYS-307; CYS-324 AND CYS-385, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=0.25 mM for alpha-D-glucosamine 1-phosphate3 Publications
Manual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional protein glmU from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes."
Pompeo F., van Heijenoort J., Mengin-Lecreulx D.
J. Bacteriol. 180:4799-4803(1998) [PubMed] [Europe PMC] [Abstract]Cited for: MUTAGENESIS OF CYS-296; CYS-307; CYS-324 AND CYS-385, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=0.32 mM for acetyl-CoA3 Publications
Manual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional protein glmU from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes."
Pompeo F., van Heijenoort J., Mengin-Lecreulx D.
J. Bacteriol. 180:4799-4803(1998) [PubMed] [Europe PMC] [Abstract]Cited for: MUTAGENESIS OF CYS-296; CYS-307; CYS-324 AND CYS-385, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=0.6 mM for acetyl-CoA3 Publications
Manual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional protein glmU from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes."
Pompeo F., van Heijenoort J., Mengin-Lecreulx D.
J. Bacteriol. 180:4799-4803(1998) [PubMed] [Europe PMC] [Abstract]Cited for: MUTAGENESIS OF CYS-296; CYS-307; CYS-324 AND CYS-385, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=0.84 mM for n-propionyl-CoA3 Publications
Manual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional protein glmU from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes."
Pompeo F., van Heijenoort J., Mengin-Lecreulx D.
J. Bacteriol. 180:4799-4803(1998) [PubMed] [Europe PMC] [Abstract]Cited for: MUTAGENESIS OF CYS-296; CYS-307; CYS-324 AND CYS-385, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=1.3 mM for UDP-glucosamine3 Publications
Manual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional protein glmU from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes."
Pompeo F., van Heijenoort J., Mengin-Lecreulx D.
J. Bacteriol. 180:4799-4803(1998) [PubMed] [Europe PMC] [Abstract]Cited for: MUTAGENESIS OF CYS-296; CYS-307; CYS-324 AND CYS-385, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=2 mM for glucose-1-P3 Publications
Manual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional protein glmU from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes."
Pompeo F., van Heijenoort J., Mengin-Lecreulx D.
J. Bacteriol. 180:4799-4803(1998) [PubMed] [Europe PMC] [Abstract]Cited for: MUTAGENESIS OF CYS-296; CYS-307; CYS-324 AND CYS-385, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=3.7 mM for N-acetylgalactosamine-1-P3 Publications
Manual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional protein glmU from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes."
Pompeo F., van Heijenoort J., Mengin-Lecreulx D.
J. Bacteriol. 180:4799-4803(1998) [PubMed] [Europe PMC] [Abstract]Cited for: MUTAGENESIS OF CYS-296; CYS-307; CYS-324 AND CYS-385, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=15 mM for galactosamine-1-phosphate3 Publications
Manual assertion based on experiment ini
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional protein glmU from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes."
Pompeo F., van Heijenoort J., Mengin-Lecreulx D.
J. Bacteriol. 180:4799-4803(1998) [PubMed] [Europe PMC] [Abstract]Cited for: MUTAGENESIS OF CYS-296; CYS-307; CYS-324 AND CYS-385, BIOPHYSICOCHEMICAL PROPERTIES.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis
This protein is involved in step 2 of the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II).UniRule annotationManual assertion according to rulesi
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II), the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.
Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis
This protein is involved in step 1 of the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate.UniRule annotationManual assertion according to rulesi
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate, the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.
Pathwayi: LPS lipid A biosynthesis
This protein is involved in the pathway LPS lipid A biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotationManual assertion according to rulesi
View all proteins of this organism that are known to be involved in the pathway LPS lipid A biosynthesis and in Bacterial outer membrane biogenesis.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 25 | UDP-GlcNAcUniRule annotation Manual assertion according to rulesi | 1 | |
| Binding sitei | 76 | UDP-GlcNAcUniRule annotation Manual assertion according to rulesi 3 PublicationsManual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 105 | CobaltCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 105 | MagnesiumCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 140 | UDP-GlcNAc; via amide nitrogenUniRule annotation Manual assertion according to rulesi 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 154 | UDP-GlcNAcUniRule annotation Manual assertion according to rulesi 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 169 | UDP-GlcNAcUniRule annotation Manual assertion according to rulesi 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 227 | CobaltCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 227 | MagnesiumCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 227 | UDP-GlcNAcUniRule annotation Manual assertion according to rulesi | 1 | |
| Binding sitei | 333 | UDP-GlcNAcUniRule annotation Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 351 | UDP-GlcNAcUniRule annotation Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 363 | Proton acceptorUniRule annotation Manual assertion according to rulesi | 1 | |
| Binding sitei | 366 | UDP-GlcNAcUniRule annotation Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 377 | UDP-GlcNAcUniRule annotation Manual assertion according to rulesi 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 380 | Acetyl-CoA; via amide nitrogenUniRule annotation Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 405 | Acetyl-CoAUniRule annotation Manual assertion according to rulesi 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 423 | Acetyl-CoA; via amide nitrogenUniRule annotation Manual assertion according to rulesi 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 440 | Acetyl-CoAUniRule annotation Manual assertion according to rulesi 3 PublicationsManual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- glucosamine-1-phosphate N-acetyltransferase activity Source: EcoCyc
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION.
- identical protein binding Source: EcoCycInferred from direct assayi
- "Self-association studies of the bifunctional N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli."
Trempe J.F., Shenker S., Kozlov G., Gehring K.
Protein Sci 20:745-752(2011) [PubMed] [Europe PMC] [Abstract]
- magnesium ion binding Source: EcoCycInferred from direct assayi
- Ref.6"Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION.
- UDP-N-acetylglucosamine diphosphorylase activity Source: EcoCycInferred from direct assayi
- Ref.7"Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
GO - Biological processi
- cell morphogenesis Source: UniProtKB-UniRule
- cell wall organization Source: UniProtKB-KW
- lipid A biosynthetic process Source: UniProtKB-UniPathway
- peptidoglycan biosynthetic process Source: UniProtKB-UniRule
- regulation of cell shape Source: UniProtKB-KW
- UDP-N-acetylglucosamine biosynthetic process Source: EcoCyc
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- Ref.5"Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli."
Mengin-Lecreulx D., van Heijenoort J.
J. Bacteriol. 175:6150-6157(1993) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Acyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Transferase |
| Biological process | Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis |
| Ligand | Cobalt, Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:NAG1P-URIDYLTRANS-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.3.1.157, 2026 2.7.7.23, 2026 |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P0ACC7 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00113;UER00532 UPA00113;UER00533 UPA00973 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Bifunctional protein GlmUUniRule annotationManual assertion according to rulesi Including the following 2 domains: UDP-N-acetylglucosamine pyrophosphorylaseUniRule annotation Manual assertion according to rulesi (EC:2.7.7.23
Manual assertion according to rulesi 3 PublicationsManual assertion based on experiment ini
Alternative name(s): N-acetylglucosamine-1-phosphate uridyltransferaseUniRule annotation Manual assertion according to rulesi Glucosamine-1-phosphate N-acetyltransferaseUniRule annotation Manual assertion according to rulesi (EC:2.3.1.157
Manual assertion according to rulesi 3 PublicationsManual assertion based on experiment ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:glmUUniRule annotation Manual assertion according to rulesi Synonyms:yieA Ordered Locus Names:b3730, JW3708 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Escherichia coli (strain K12) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 83333 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation
Manual assertion according to rulesi
1 PublicationManual assertion based on experiment ini
- Ref.9"Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily."
Brown K., Pompeo F., Dixon S., Mengin-Lecreulx D., Cambillau C., Bourne Y.
EMBO J. 18:4096-4107(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF THE TRUNCATED FORM AND IN COMPLEX WITH UDP-GLCNAC, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-14; ARG-18 AND LYS-25, SUBCELLULAR LOCATION, SUBUNIT.
- Cytoplasm UniRule annotation
Cytosol
- cytosol Source: EcoCycInferred from direct assayi
- "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth."
Lopez-Campistrous A., Semchuk P., Burke L., Palmer-Stone T., Brokx S.J., Broderick G., Bottorff D., Bolch S., Weiner J.H., Ellison M.J.
Mol. Cell. Proteomics 4:1205-1209(2005) [PubMed] [Europe PMC] [Abstract] - "Protein abundance profiling of the Escherichia coli cytosol."
Ishihama Y., Schmidt T., Rappsilber J., Mann M., Hartl F.U., Kerner M.J., Frishman D.
BMC Genomics 9:102-102(2008) [PubMed] [Europe PMC] [Abstract]
- cytosol Source: EcoCycInferred from direct assayi
Keywords - Cellular componenti
Cytoplasm<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 14 | G → A: 8-fold decrease in uridyltransferase activity. Creates steric conflict and decreases affinity for UTP. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 18 | R → A: Dramatically impairs the uridyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 25 | K → A: 8-fold decrease in uridyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 296 | C → A: No effect. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 307 | C → A: 1350-fold decrease in acetyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 324 | C → A: 8-fold decrease in acetyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 385 | C → A: No effect. 1 Publication Manual assertion based on experiment ini
| 1 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3414415 |
Drug and drug target database More...DrugBanki | DB03814, 2-(N-morpholino)ethanesulfonic acid DB01992, Coenzyme A DB03397, Uridine-Diphosphate-N-Acetylglucosamine |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000068701 | 1 – 456 | Bifunctional protein GlmUAdd BLAST | 456 |
Proteomic databases
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P0ACC7 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0ACC7 |
PRoteomics IDEntifications database More...PRIDEi | P0ACC7 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homotrimer. In vivo forms a hexameric aggregate.
5 PublicationsManual assertion based on experiment ini
- Ref.9"Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily."
Brown K., Pompeo F., Dixon S., Mengin-Lecreulx D., Cambillau C., Bourne Y.
EMBO J. 18:4096-4107(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF THE TRUNCATED FORM AND IN COMPLEX WITH UDP-GLCNAC, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-14; ARG-18 AND LYS-25, SUBCELLULAR LOCATION, SUBUNIT. - Ref.10"Structure of the Escherichia coli glmU pyrophosphorylase and acetyltransferase active sites."
Olsen L.R., Roderick S.L.
Biochemistry 40:1913-1921(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC; COA AND COBALT ION, COFACTOR, SUBUNIT. - Ref.11"Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products."
Olsen L.R., Vetting M.W., Roderick S.L.
Protein Sci. 16:1230-1235(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC, COA AND MAGNESIUM IONS, COFACTOR, SUBUNIT. - Ref.12"In vitro validation of acetyltransferase activity of GlmU as an antibacterial target in Haemophilus influenzae."
Buurman E.T., Andrews B., Gao N., Hu J., Keating T.A., Lahiri S., Otterbein L.R., Patten A.D., Stokes S.S., Shapiro A.B.
J. Biol. Chem. 286:40734-40742(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 233-452 ACETYL-COA ANALOG, FUNCTION, ACTIVITY REGULATION, SUBUNIT. - Ref.13"Inhibitors of acetyltransferase domain of N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU). Part 1: Hit to lead evaluation of a novel arylsulfonamide series."
Green O.M., McKenzie A.R., Shapiro A.B., Otterbein L., Ni H., Patten A., Stokes S., Albert R., Kawatkar S., Breed J.
Bioorg. Med. Chem. Lett. 22:1510-1519(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 227-456, FUNCTION, ACTIVITY REGULATION, SUBUNIT.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
P0ACC7
| With | #Exp. | IntAct |
|---|---|---|
| rpsB [P0A7V0] | 2 | EBI-370256,EBI-543439 |
GO - Molecular functioni
- identical protein binding Source: EcoCycInferred from direct assayi
- "Self-association studies of the bifunctional N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli."
Trempe J.F., Shenker S., Kozlov G., Gehring K.
Protein Sci 20:745-752(2011) [PubMed] [Europe PMC] [Abstract]
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 4262143, 312 interactors 852548, 1 interactor |
Database of interacting proteins More...DIPi | DIP-31844N |
Protein interaction database and analysis system More...IntActi | P0ACC7, 19 interactors |
STRING: functional protein association networks More...STRINGi | 511145.b3730 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P0ACC7 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 6 – 12 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 17 – 19 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 25 – 27 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 28 – 30 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 35 – 46 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
| Beta strandi | 51 – 55 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 59 – 65 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 66 – 68 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 71 – 75 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 82 – 89 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 90 – 92 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 97 – 103 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 111 – 120 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 125 – 132 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 141 – 145 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 148 – 153 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Turni | 155 – 157 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 162 – 164 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 167 – 176 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 177 – 184 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 191 – 193 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 198 – 200 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 201 – 206 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Turni | 207 – 209 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 212 – 215 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 220 – 223 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 233 – 249 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 17 | |
| Beta strandi | 253 – 255 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 257 – 259 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 260 – 268 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 278 – 286 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 297 – 300 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 314 – 317 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 325 – 327 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 328 – 332 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 336 – 338 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 343 – 355 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
| Beta strandi | 360 – 372 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
| Beta strandi | 383 – 385 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 387 – 390 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 395 – 397 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 408 – 415 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0ACC7 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P0ACC7 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1 – 229 | PyrophosphorylaseUniRule annotation Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 229 | |
| Regioni | 11 – 14 | UDP-GlcNAc bindingUniRule annotation Manual assertion according to rulesi 3 PublicationsManual assertion based on experiment ini
| 4 | |
| Regioni | 81 – 82 | UDP-GlcNAc bindingUniRule annotation Manual assertion according to rulesi 3 PublicationsManual assertion based on experiment ini
| 2 | |
| Regioni | 103 – 105 | UDP-GlcNAc bindingUniRule annotation Manual assertion according to rulesi 3 PublicationsManual assertion based on experiment ini
| 3 | |
| Regioni | 230 – 250 | LinkerUniRule annotation Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 21 | |
| Regioni | 251 – 456 | N-acetyltransferaseUniRule annotation Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 206 | |
| Regioni | 386 – 387 | Acetyl-CoA bindingUniRule annotation Manual assertion according to rulesi | 2 |
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.UniRule annotation
Manual assertion according to rulesi
CuratedIn the C-terminal section; belongs to the transferase hexapeptide repeat family.UniRule annotation
Manual assertion according to rulesi
CuratedKeywords - Domaini
RepeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG1207, Bacteria |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_029499_15_2_6 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0ACC7 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0ACC7 |
Family and domain databases
Conserved Domains Database More...CDDi | cd03353, LbH_GlmU_C, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.90.550.10, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_01631, GlmU, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005882, Bifunctional_GlmU IPR038009, GlmU_C_LbH IPR001451, Hexapep IPR018357, Hexapep_transf_CS IPR025877, MobA-like_NTP_Trfase IPR029044, Nucleotide-diphossugar_trans IPR011004, Trimer_LpxA-like_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF00132, Hexapep, 2 hits PF14602, Hexapep_2, 1 hit PF12804, NTP_transf_3, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51161, SSF51161, 1 hit SSF53448, SSF53448, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01173, glmU, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00101, HEXAPEP_TRANSFERASES, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
P0ACC7-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MLNNAMSVVI LAAGKGTRMY SDLPKVLHTL AGKAMVQHVI DAANELGAAH
60 70 80 90 100
VHLVYGHGGD LLKQALKDDN LNWVLQAEQL GTGHAMQQAA PFFADDEDIL
110 120 130 140 150
MLYGDVPLIS VETLQRLRDA KPQGGIGLLT VKLDDPTGYG RITRENGKVT
160 170 180 190 200
GIVEHKDATD EQRQIQEINT GILIANGADM KRWLAKLTNN NAQGEYYITD
210 220 230 240 250
IIALAYQEGR EIVAVHPQRL SEVEGVNNRL QLSRLERVYQ SEQAEKLLLA
260 270 280 290 300
GVMLRDPARF DLRGTLTHGR DVEIDTNVII EGNVTLGHRV KIGTGCVIKN
310 320 330 340 350
SVIGDDCEIS PYTVVEDANL AAACTIGPFA RLRPGAELLE GAHVGNFVEM
360 370 380 390 400
KKARLGKGSK AGHLTYLGDA EIGDNVNIGA GTITCNYDGA NKFKTIIGDD
410 420 430 440 450
VFVGSDTQLV APVTVGKGAT IAAGTTVTRN VGENALAISR VPQTQKEGWR
RPVKKK
Length:456
Mass (Da):49,190
Last modified:November 8, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i2F3C5C84F673C8A3
<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 186 – 187 | KL → NV in CAA25784 (PubMed:6395859).Curated | 2 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X01631 Genomic DNA Translation: CAA25784.1 L10328 Genomic DNA Translation: AAA62082.1 Frameshift. L10328 Genomic DNA Translation: AAA62081.1 Frameshift. U00096 Genomic DNA Translation: AAC76753.1 AP009048 Genomic DNA Translation: BAE77558.1 |
Protein sequence database of the Protein Information Resource More...PIRi | C65176 |
NCBI Reference Sequences More...RefSeqi | NP_418186.1, NC_000913.3 WP_000933736.1, NZ_STEB01000015.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC76753; AAC76753; b3730 BAE77558; BAE77558; BAE77558 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 66672366 948246 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW3708 eco:b3730 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.2970 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P0ACC7 | Bifunctional protein GlmU | 456 | UniRef100_A7ZTU1 | |||
| Bifunctional protein GlmU | 456 | |||||
| Bifunctional protein GlmU | 456 | |||||
| Bifunctional protein GlmU | 456 | |||||
| Bifunctional protein GlmU | 456 | |||||
| +152 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P0ACC7 | Bifunctional protein GlmU | 456 | UniRef90_A4WGF8 | |||
| Bifunctional protein GlmU | 456 | |||||
| Bifunctional protein GlmU | 456 | |||||
| Bifunctional protein GlmU | 456 | |||||
| Bifunctional protein GlmU | 456 | |||||
| +1520 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P0ACC7 | Bifunctional protein GlmU | 456 | UniRef50_A7MMY0 | |||
| Bifunctional protein GlmU | 457 | |||||
| Bifunctional protein GlmU | 454 | |||||
| Bifunctional protein GlmU | 457 | |||||
| Bifunctional protein GlmU | 457 | |||||
| +6452 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X01631 Genomic DNA Translation: CAA25784.1 L10328 Genomic DNA Translation: AAA62082.1 Frameshift. L10328 Genomic DNA Translation: AAA62081.1 Frameshift. U00096 Genomic DNA Translation: AAC76753.1 AP009048 Genomic DNA Translation: BAE77558.1 |
| PIRi | C65176 |
| RefSeqi | NP_418186.1, NC_000913.3 WP_000933736.1, NZ_STEB01000015.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1FWY | X-ray | 2.30 | A/B | 1-331 | [»] | |
| 1FXJ | X-ray | 2.25 | A/B | 1-331 | [»] | |
| 1HV9 | X-ray | 2.10 | A/B | 1-456 | [»] | |
| 2OI5 | X-ray | 2.25 | A/B | 1-456 | [»] | |
| 2OI6 | X-ray | 2.20 | A/B | 1-456 | [»] | |
| 2OI7 | X-ray | 2.54 | A/B | 1-456 | [»] | |
| 3TWD | X-ray | 1.90 | A/B | 233-452 | [»] | |
| 4AA7 | X-ray | 2.00 | A/B | 227-456 | [»] | |
| SMRi | P0ACC7 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| BioGRIDi | 4262143, 312 interactors 852548, 1 interactor |
| DIPi | DIP-31844N |
| IntActi | P0ACC7, 19 interactors |
| STRINGi | 511145.b3730 |
Chemistry databases
| BindingDBi | P0ACC7 |
| ChEMBLi | CHEMBL3414415 |
| DrugBanki | DB03814, 2-(N-morpholino)ethanesulfonic acid DB01992, Coenzyme A DB03397, Uridine-Diphosphate-N-Acetylglucosamine |
Proteomic databases
| jPOSTi | P0ACC7 |
| PaxDbi | P0ACC7 |
| PRIDEi | P0ACC7 |
Genome annotation databases
| EnsemblBacteriai | AAC76753; AAC76753; b3730 BAE77558; BAE77558; BAE77558 |
| GeneIDi | 66672366 948246 |
| KEGGi | ecj:JW3708 eco:b3730 |
| PATRICi | fig|1411691.4.peg.2970 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB1184 |
Phylogenomic databases
| eggNOGi | COG1207, Bacteria |
| HOGENOMi | CLU_029499_15_2_6 |
| InParanoidi | P0ACC7 |
| PhylomeDBi | P0ACC7 |
Enzyme and pathway databases
| UniPathwayi | UPA00113;UER00532 UPA00113;UER00533 UPA00973 |
| BioCyci | EcoCyc:NAG1P-URIDYLTRANS-MONOMER |
| BRENDAi | 2.3.1.157, 2026 2.7.7.23, 2026 |
| SABIO-RKi | P0ACC7 |
Miscellaneous databases
| EvolutionaryTracei | P0ACC7 |
Protein Ontology More...PROi | PR:P0ACC7 |
Family and domain databases
| CDDi | cd03353, LbH_GlmU_C, 1 hit |
| Gene3Di | 3.90.550.10, 1 hit |
| HAMAPi | MF_01631, GlmU, 1 hit |
| InterProi | View protein in InterPro IPR005882, Bifunctional_GlmU IPR038009, GlmU_C_LbH IPR001451, Hexapep IPR018357, Hexapep_transf_CS IPR025877, MobA-like_NTP_Trfase IPR029044, Nucleotide-diphossugar_trans IPR011004, Trimer_LpxA-like_sf |
| Pfami | View protein in Pfam PF00132, Hexapep, 2 hits PF14602, Hexapep_2, 1 hit PF12804, NTP_transf_3, 1 hit |
| SUPFAMi | SSF51161, SSF51161, 1 hit SSF53448, SSF53448, 1 hit |
| TIGRFAMsi | TIGR01173, glmU, 1 hit |
| PROSITEi | View protein in PROSITE PS00101, HEXAPEP_TRANSFERASES, 1 hit |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | GLMU_ECOLI | |
| <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P0ACC7Primary (citable) accession number: P0ACC7 Secondary accession number(s): P17114, P76746, Q2M848 | |
| <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 8, 2005 |
| Last sequence update: | November 8, 2005 | |
| Last modified: | February 23, 2022 | |
| This is version 138 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
