UniProtKB - P0AF12 (MTNN_ECOLI)
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- BLAST>sp|P0AF12|MTNN_ECOLI 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase OS=Escherichia coli (strain K12) OX=83333 GN=mtnN PE=1 SV=1 MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGAT LLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFK ADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAH VCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG
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5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
mtnN
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
<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.10"Mutational analysis of a nucleosidase involved in quorum-sensing autoinducer-2 biosynthesis."
Lee J.E., Luong W., Huang D.J., Cornell K.A., Riscoe M.K., Howell P.L.
Biochemistry 44:11049-11057(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF MET-9; GLU-12; ILE-50; SER-76; PHE-151; MET-173; GLU-174; ARG-193; SER-196; ASP-197 AND PHE-207.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<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.10"Mutational analysis of a nucleosidase involved in quorum-sensing autoinducer-2 biosynthesis."
Lee J.E., Luong W., Huang D.J., Cornell K.A., Riscoe M.K., Howell P.L.
Biochemistry 44:11049-11057(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF MET-9; GLU-12; ILE-50; SER-76; PHE-151; MET-173; GLU-174; ARG-193; SER-196; ASP-197 AND PHE-207.
<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.10"Mutational analysis of a nucleosidase involved in quorum-sensing autoinducer-2 biosynthesis."
Lee J.E., Luong W., Huang D.J., Cornell K.A., Riscoe M.K., Howell P.L.
Biochemistry 44:11049-11057(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF MET-9; GLU-12; ILE-50; SER-76; PHE-151; MET-173; GLU-174; ARG-193; SER-196; ASP-197 AND PHE-207.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<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.7"Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Purification, substrate specificity and mechanism of action."
Della Ragione F., Porcelli M., Carteni-Farina M., Zappia V., Pegg A.E.
Biochem. J. 232:335-341(1985) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.8"Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: analysis of enzymatic activity and substrate specificity."
Cornell K.A., Swarts W.E., Barry R.D., Riscoe M.K.
Biochem. Biophys. Res. Commun. 228:724-732(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.12"Structure of Escherichia coli 5'-methylthioadenosine/ S-adenosylhomocysteine nucleosidase inhibitor complexes provide insight into the conformational changes required for substrate binding and catalysis."
Lee J.E., Cornell K.A., Riscoe M.K., Howell P.L.
J. Biol. Chem. 278:8761-8770(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, ENZYME REGULATION. - Ref.13"Femtomolar transition state analogue inhibitors of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Escherichia coli."
Singh V., Evans G.B., Lenz D.H., Mason J.M., Clinch K., Mee S., Painter G.F., Tyler P.C., Furneaux R.H., Lee J.E., Howell P.L., Schramm V.L.
J. Biol. Chem. 280:18265-18273(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, ENZYME REGULATION.
<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
<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.10"Mutational analysis of a nucleosidase involved in quorum-sensing autoinducer-2 biosynthesis."
Lee J.E., Luong W., Huang D.J., Cornell K.A., Riscoe M.K., Howell P.L.
Biochemistry 44:11049-11057(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF MET-9; GLU-12; ILE-50; SER-76; PHE-151; MET-173; GLU-174; ARG-193; SER-196; ASP-197 AND PHE-207.
- KM=0.43 µM for 5'-methylthioadenosine (at pH 7 and 37 degrees Celsius)3 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.7"Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Purification, substrate specificity and mechanism of action."
Della Ragione F., Porcelli M., Carteni-Farina M., Zappia V., Pegg A.E.
Biochem. J. 232:335-341(1985) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.8"Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: analysis of enzymatic activity and substrate specificity."
Cornell K.A., Swarts W.E., Barry R.D., Riscoe M.K.
Biochem. Biophys. Res. Commun. 228:724-732(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.10"Mutational analysis of a nucleosidase involved in quorum-sensing autoinducer-2 biosynthesis."
Lee J.E., Luong W., Huang D.J., Cornell K.A., Riscoe M.K., Howell P.L.
Biochemistry 44:11049-11057(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF MET-9; GLU-12; ILE-50; SER-76; PHE-151; MET-173; GLU-174; ARG-193; SER-196; ASP-197 AND PHE-207.
- KM=0.8 µM for 5'-methylthioadenosine (at pH 7 and 22 degrees Celsius)3 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.7"Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Purification, substrate specificity and mechanism of action."
Della Ragione F., Porcelli M., Carteni-Farina M., Zappia V., Pegg A.E.
Biochem. J. 232:335-341(1985) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.8"Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: analysis of enzymatic activity and substrate specificity."
Cornell K.A., Swarts W.E., Barry R.D., Riscoe M.K.
Biochem. Biophys. Res. Commun. 228:724-732(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.10"Mutational analysis of a nucleosidase involved in quorum-sensing autoinducer-2 biosynthesis."
Lee J.E., Luong W., Huang D.J., Cornell K.A., Riscoe M.K., Howell P.L.
Biochemistry 44:11049-11057(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF MET-9; GLU-12; ILE-50; SER-76; PHE-151; MET-173; GLU-174; ARG-193; SER-196; ASP-197 AND PHE-207.
- KM=4.3 µM for S-adenosylhomocysteine (at pH 7 and 37 degrees Celsius)3 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.7"Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Purification, substrate specificity and mechanism of action."
Della Ragione F., Porcelli M., Carteni-Farina M., Zappia V., Pegg A.E.
Biochem. J. 232:335-341(1985) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.8"Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: analysis of enzymatic activity and substrate specificity."
Cornell K.A., Swarts W.E., Barry R.D., Riscoe M.K.
Biochem. Biophys. Res. Commun. 228:724-732(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.10"Mutational analysis of a nucleosidase involved in quorum-sensing autoinducer-2 biosynthesis."
Lee J.E., Luong W., Huang D.J., Cornell K.A., Riscoe M.K., Howell P.L.
Biochemistry 44:11049-11057(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF MET-9; GLU-12; ILE-50; SER-76; PHE-151; MET-173; GLU-174; ARG-193; SER-196; ASP-197 AND PHE-207.
- KM=1.3 µM for S-adenosylhomocysteine (at pH 7 and 22 degrees Celsius)3 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.7"Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Purification, substrate specificity and mechanism of action."
Della Ragione F., Porcelli M., Carteni-Farina M., Zappia V., Pegg A.E.
Biochem. J. 232:335-341(1985) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.8"Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: analysis of enzymatic activity and substrate specificity."
Cornell K.A., Swarts W.E., Barry R.D., Riscoe M.K.
Biochem. Biophys. Res. Commun. 228:724-732(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.10"Mutational analysis of a nucleosidase involved in quorum-sensing autoinducer-2 biosynthesis."
Lee J.E., Luong W., Huang D.J., Cornell K.A., Riscoe M.K., Howell P.L.
Biochemistry 44:11049-11057(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF MET-9; GLU-12; ILE-50; SER-76; PHE-151; MET-173; GLU-174; ARG-193; SER-196; ASP-197 AND PHE-207.
- Vmax=373 µmol/min/mg enzyme with 5'-methylthioadenosine as substrate (at pH 7 and 37 degrees Celsius)3 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.7"Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Purification, substrate specificity and mechanism of action."
Della Ragione F., Porcelli M., Carteni-Farina M., Zappia V., Pegg A.E.
Biochem. J. 232:335-341(1985) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.8"Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: analysis of enzymatic activity and substrate specificity."
Cornell K.A., Swarts W.E., Barry R.D., Riscoe M.K.
Biochem. Biophys. Res. Commun. 228:724-732(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.10"Mutational analysis of a nucleosidase involved in quorum-sensing autoinducer-2 biosynthesis."
Lee J.E., Luong W., Huang D.J., Cornell K.A., Riscoe M.K., Howell P.L.
Biochemistry 44:11049-11057(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF MET-9; GLU-12; ILE-50; SER-76; PHE-151; MET-173; GLU-174; ARG-193; SER-196; ASP-197 AND PHE-207.
- Vmax=156 µmol/min/mg enzyme with S-adenosylhomocysteine as substrate (at pH 7 and 37 degrees Celsius)3 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.7"Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Purification, substrate specificity and mechanism of action."
Della Ragione F., Porcelli M., Carteni-Farina M., Zappia V., Pegg A.E.
Biochem. J. 232:335-341(1985) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.8"Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: analysis of enzymatic activity and substrate specificity."
Cornell K.A., Swarts W.E., Barry R.D., Riscoe M.K.
Biochem. Biophys. Res. Commun. 228:724-732(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.10"Mutational analysis of a nucleosidase involved in quorum-sensing autoinducer-2 biosynthesis."
Lee J.E., Luong W., Huang D.J., Cornell K.A., Riscoe M.K., Howell P.L.
Biochemistry 44:11049-11057(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF MET-9; GLU-12; ILE-50; SER-76; PHE-151; MET-173; GLU-174; ARG-193; SER-196; ASP-197 AND PHE-207.
<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>pH dependencei
<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.7"Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Purification, substrate specificity and mechanism of action."
Della Ragione F., Porcelli M., Carteni-Farina M., Zappia V., Pegg A.E.
Biochem. J. 232:335-341(1985) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.8"Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: analysis of enzymatic activity and substrate specificity."
Cornell K.A., Swarts W.E., Barry R.D., Riscoe M.K.
Biochem. Biophys. Res. Commun. 228:724-732(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
<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>Temperature dependencei
<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.7"Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Purification, substrate specificity and mechanism of action."
Della Ragione F., Porcelli M., Carteni-Farina M., Zappia V., Pegg A.E.
Biochem. J. 232:335-341(1985) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. - Ref.8"Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: analysis of enzymatic activity and substrate specificity."
Cornell K.A., Swarts W.E., Barry R.D., Riscoe M.K.
Biochem. Biophys. Res. Commun. 228:724-732(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-methionine biosynthesis via salvage pathway
This protein is involved in step 1 of the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route).Proteins known to be involved in the 2 steps of the subpathway in this organism are:
- 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (mtnN)
- no protein annotated in this organism
View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route), the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ 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 | 12 | Proton acceptor1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the ‘Function’ 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 | 78 | Substrate; via amide nitrogen1 Publication <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
| 1 | |
| <p>This subsection of the ‘Function’ 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 | 152 | Substrate; via amide nitrogen and carbonyl oxygen1 Publication <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
| 1 | |
| <p>This subsection of the ‘Function’ 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 | 197 | Proton donor1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 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
- adenosylhomocysteine nucleosidase 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
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- methylthioadenosine nucleosidase 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
<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 - Biological processi
- L-methionine salvage from methylthioadenosine Source: UniProtKB-UniPathway
- L-methionine salvage from S-adenosylmethionine 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
- nucleoside catabolic process Source: InterPro
<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 | Hydrolase |
| Biological process | Amino-acid biosynthesis, Methionine biosynthesis |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG11090-MONOMER MetaCyc:EG11090-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.2.2.30 2026 3.2.2.9 2026 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00904; UER00871 |
<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_and_taxonomy_section">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: 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (EC:3.2.2.9)Short name: MTA/SAH nucleosidase Short name: MTAN Alternative name(s): 5'-methylthioadenosine nucleosidase Short name: MTA nucleosidase P46 S-adenosylhomocysteine nucleosidase Short name: AdoHcy nucleosidase Short name: SAH nucleosidase Short name: SRH nucleosidase |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:mtnN Synonyms:mtn, pfs, yadA Ordered Locus Names:b0159, JW0155 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 |
|
Organism-specific databases
Escherichia coli strain K12 genome database More...EcoGenei | EG11090 pfs |
<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
<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 - Cellular componenti
- cytosol 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
<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_and_biotech_section">'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 | 9 | M → A: 13-19% of wild-type catalytic efficiency. 1 Publication <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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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 | 12 | E → A or Q: Loss of catalytic activity. 1 Publication <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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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 | 50 | I → A: 12-23% of wild-type catalytic efficiency. 1 Publication <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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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 | 76 | S → A: 13-23% of wild-type catalytic efficiency. 1 Publication <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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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 | 151 | F → A: 0.5% of wild-type catalytic efficiency. 1 Publication <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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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 | 173 | M → A: 0.5% of wild-type catalytic efficiency. 1 Publication <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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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 | 174 | E → A or Q: Loss of catalytic activity. 1 Publication <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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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 | 193 | R → A: 13-28% of wild-type catalytic efficiency. 1 Publication <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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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 | 196 | S → A: 2-4% of wild-type catalytic efficiency. 1 Publication <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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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 | 197 | D → A or N: Loss of catalytic activity. 1 Publication <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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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 | 207 | F → A: 2% of wild-type catalytic efficiency. 1 Publication <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
| 1 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2866 |
Drug and drug target database More...DrugBanki | DB02933 5'-Deoxy-5'-(Methylthio)-Tubercidin DB00173 Adenine DB02281 Formycin |
<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000164439 | 1 – 232 | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidaseAdd BLAST | 232 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P0AF12 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0AF12 |
PRoteomics IDEntifications database More...PRIDEi | P0AF12 |
2D gel databases
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P0AF12 |
<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<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.11"Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases."
Lee J.E., Cornell K.A., Riscoe M.K., Howell P.L.
Structure 9:941-953(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT. - Ref.12"Structure of Escherichia coli 5'-methylthioadenosine/ S-adenosylhomocysteine nucleosidase inhibitor complexes provide insight into the conformational changes required for substrate binding and catalysis."
Lee J.E., Cornell K.A., Riscoe M.K., Howell P.L.
J. Biol. Chem. 278:8761-8770(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, ENZYME REGULATION. - Ref.13"Femtomolar transition state analogue inhibitors of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Escherichia coli."
Singh V., Evans G.B., Lenz D.H., Mason J.M., Clinch K., Mee S., Painter G.F., Tyler P.C., Furneaux R.H., Lee J.E., Howell P.L., Schramm V.L.
J. Biol. Chem. 280:18265-18273(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, ENZYME REGULATION. - Ref.14"Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis."
Lee J.E., Smith G.D., Horvatin C., Huang D.J., Cornell K.A., Riscoe M.K., Howell P.L.
J. Mol. Biol. 352:559-574(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF WILD-TYPE AND MUTANTS ASN-197 AND GLN-12 IN COMPLEX WITH MTA SUBSTRATE OR PRODUCTS, REACTION MECHANISM, ACTIVE SITES.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| itself | 2 | EBI-1114261,EBI-1114261 |
<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
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 4260991, 38 interactors |
Database of interacting proteins More...DIPi | DIP-10270N |
Protein interaction database and analysis system More...IntActi | P0AF12, 7 interactors |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_0139 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P0AF12 |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ 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 | 2 – 9 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ 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 | 10 – 17 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ 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 | 21 – 28 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ 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 | 31 – 38 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ 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 | 41 – 47 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ 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 | 52 – 66 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ 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 | 69 – 79 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ 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 | 89 – 99 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ 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 | 103 – 105 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ 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 | 117 – 120 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ 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 | 123 – 135 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ 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 | 140 – 147 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ 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 | 155 – 164 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ 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 | 168 – 174 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ 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 | 175 – 185 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ 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 | 189 – 197 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ 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 | 203 – 231 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 29 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P0AF12 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0AF12 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P0AF12 |
<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 | 173 – 174 | Substrate binding | 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
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4105DUF Bacteria COG0775 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000259346 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0AF12 |
KEGG Orthology (KO) More...KOi | K01243 |
Identification of Orthologs from Complete Genome Data More...OMAi | DQFVHSK |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0AF12 |
Family and domain databases
HAMAP database of protein families More...HAMAPi | MF_01684 Salvage_MtnN, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR010049 MTA_SAH_Nsdase IPR000845 Nucleoside_phosphorylase_d IPR035994 Nucleoside_phosphorylase_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF01048 PNP_UDP_1, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53167 SSF53167, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01704 MTA/SAH-Nsdase, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.
10 20 30 40 50
MKIGIIGAME EEVTLLRDKI ENRQTISLGG CEIYTGQLNG TEVALLKSGI
60 70 80 90 100
GKVAAALGAT LLLEHCKPDV IINTGSAGGL APTLKVGDIV VSDEARYHDA
110 120 130 140 150
DVTAFGYEYG QLPGCPAGFK ADDKLIAAAE ACIAELNLNA VRGLIVSGDA
160 170 180 190 200
FINGSVGLAK IRHNFPQAIA VEMEATAIAH VCHNFNVPFV VVRAISDVAD
210 220 230
QQSHLSFDEF LAVAAKQSSL MVESLVQKLA HG
<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 | 212 – 232 | AVAAK…KLAHG → LLPLNSPA in AAA23678 (PubMed:2157212).CuratedAdd BLAST | 21 | |
| <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 | 212 – 232 | AVAAK…KLAHG → LLPLNSPA in AAA24322 (PubMed:2157212).CuratedAdd BLAST | 21 |
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 | M31772 Genomic DNA Translation: AAA23678.1 Different initiation. U24438 Genomic DNA Translation: AAC38291.1 M83735 Genomic DNA Translation: AAA24322.1 U70214 Genomic DNA Translation: AAB08589.1 U00096 Genomic DNA Translation: AAC73270.1 AP009048 Genomic DNA Translation: BAB96736.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S45227 |
NCBI Reference Sequences More...RefSeqi | NP_414701.1, NC_000913.3 WP_000689844.1, NZ_LN832404.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC73270; AAC73270; b0159 BAB96736; BAB96736; BAB96736 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 948542 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW0155 eco:b0159 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.2121 |
<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
<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: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M31772 Genomic DNA Translation: AAA23678.1 Different initiation. U24438 Genomic DNA Translation: AAC38291.1 M83735 Genomic DNA Translation: AAA24322.1 U70214 Genomic DNA Translation: AAB08589.1 U00096 Genomic DNA Translation: AAC73270.1 AP009048 Genomic DNA Translation: BAB96736.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S45227 |
NCBI Reference Sequences More...RefSeqi | NP_414701.1, NC_000913.3 WP_000689844.1, NZ_LN832404.1 |
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 |
| 1JYS | X-ray | 1.90 | A/B | 1-232 | [»] | |
| 1NC1 | X-ray | 2.00 | A/B | 1-232 | [»] | |
| 1NC3 | X-ray | 2.20 | A/B | 1-232 | [»] | |
| 1Y6Q | X-ray | 2.20 | A/B | 1-232 | [»] | |
| 1Y6R | X-ray | 2.20 | A/B | 1-232 | [»] | |
| 1Z5N | X-ray | 2.10 | A/B | 1-232 | [»] | |
| 1Z5O | X-ray | 2.00 | A/B | 1-232 | [»] | |
| 1Z5P | X-ray | 2.00 | A | 1-232 | [»] | |
| 3O4V | X-ray | 1.75 | A/B | 1-232 | [»] | |
| 4WKC | X-ray | 1.64 | A | 1-232 | [»] | |
| 4YML | X-ray | 1.75 | A | 1-232 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P0AF12 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0AF12 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 4260991, 38 interactors |
Database of interacting proteins More...DIPi | DIP-10270N |
Protein interaction database and analysis system More...IntActi | P0AF12, 7 interactors |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_0139 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P0AF12 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2866 |
Drug and drug target database More...DrugBanki | DB02933 5'-Deoxy-5'-(Methylthio)-Tubercidin DB00173 Adenine DB02281 Formycin |
2D gel databases
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P0AF12 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P0AF12 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0AF12 |
PRoteomics IDEntifications database More...PRIDEi | P0AF12 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC73270; AAC73270; b0159 BAB96736; BAB96736; BAB96736 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 948542 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW0155 eco:b0159 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.2121 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB1082 |
Escherichia coli strain K12 genome database More...EcoGenei | EG11090 pfs |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4105DUF Bacteria COG0775 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000259346 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0AF12 |
KEGG Orthology (KO) More...KOi | K01243 |
Identification of Orthologs from Complete Genome Data More...OMAi | DQFVHSK |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0AF12 |
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00904; UER00871 |
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG11090-MONOMER MetaCyc:EG11090-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.2.2.30 2026 3.2.2.9 2026 |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P0AF12 |
Protein Ontology More...PROi | PR:P0AF12 |
Family and domain databases
HAMAP database of protein families More...HAMAPi | MF_01684 Salvage_MtnN, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR010049 MTA_SAH_Nsdase IPR000845 Nucleoside_phosphorylase_d IPR035994 Nucleoside_phosphorylase_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF01048 PNP_UDP_1, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53167 SSF53167, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01704 MTA/SAH-Nsdase, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | 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 | MTNN_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 | P0AF12Primary (citable) accession number: P0AF12 Secondary accession number(s): P24247 | |
| <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 20, 2005 |
| Last sequence update: | December 20, 2005 | |
| Last modified: | March 28, 2018 | |
| This is version 110 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
<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>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene - 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
