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P0ACC7

- GLMU_ECOLI

UniProt

P0ACC7 - GLMU_ECOLI

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Protein

Bifunctional protein GlmU

Gene
glmU, yieA, b3730, JW3708
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 Publications

Catalytic activityi

Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.1 Publication
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine.1 Publication

Cofactori

Binds 1 magnesium ion per subunit. Can also use cobalt ions to a lesser extent.1 Publication

Enzyme 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

Kineticsi

  1. KM=0.018 mM for N-acetylglucosamine 1-phosphate3 Publications
  2. KM=0.15 mM for alpha-D-glucosamine 1-phosphate
  3. KM=0.25 mM for alpha-D-glucosamine 1-phosphate
  4. KM=0.32 mM for acetyl-CoA
  5. KM=0.6 mM for acetyl-CoA
  6. KM=0.84 mM for n-propionyl-CoA
  7. KM=1.3 mM for UDP-glucosamine
  8. KM=2 mM for glucose-1-P
  9. KM=3.7 mM for N-acetylgalactosamine-1-P
  10. KM=15 mM for galactosamine-1-phosphate

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei25 – 251UDP-GlcNAc By similarity
Binding sitei76 – 761UDP-GlcNAc
Metal bindingi105 – 1051Magnesium
Binding sitei140 – 1401UDP-GlcNAc; via amide nitrogen
Binding sitei154 – 1541UDP-GlcNAc
Binding sitei169 – 1691UDP-GlcNAc
Metal bindingi227 – 2271Magnesium
Binding sitei227 – 2271UDP-GlcNAc By similarity
Binding sitei333 – 3331UDP-GlcNAc
Binding sitei351 – 3511UDP-GlcNAc
Active sitei363 – 3631Proton acceptor By similarity
Binding sitei366 – 3661UDP-GlcNAc
Binding sitei377 – 3771UDP-GlcNAc
Binding sitei380 – 3801Acetyl-CoA; via amide nitrogen
Binding sitei405 – 4051Acetyl-CoA
Binding sitei423 – 4231Acetyl-CoA; via amide nitrogen
Binding sitei440 – 4401Acetyl-CoA

GO - Molecular functioni

  1. glucosamine-1-phosphate N-acetyltransferase activity Source: EcoCyc
  2. identical protein binding Source: EcoCyc
  3. magnesium ion binding Source: EcoCyc
  4. UDP-N-acetylglucosamine diphosphorylase activity Source: EcoCyc

GO - Biological processi

  1. cell morphogenesis Source: UniProtKB-HAMAP
  2. lipid A biosynthetic process Source: UniProtKB-UniPathway
  3. lipopolysaccharide biosynthetic process Source: InterPro
  4. peptidoglycan biosynthetic process Source: UniProtKB-HAMAP
  5. regulation of cell shape Source: UniProtKB-KW
  6. UDP-N-acetylglucosamine biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Keywords - Ligandi

Cobalt, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:NAG1P-URIDYLTRANS-MONOMER.
ECOL316407:JW3708-MONOMER.
MetaCyc:NAG1P-URIDYLTRANS-MONOMER.
UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein GlmU
Including the following 2 domains:
UDP-N-acetylglucosamine pyrophosphorylase (EC:2.7.7.23)
Alternative name(s):
N-acetylglucosamine-1-phosphate uridyltransferase
Glucosamine-1-phosphate N-acetyltransferase (EC:2.3.1.157)
Gene namesi
Name:glmU
Synonyms:yieA
Ordered Locus Names:b3730, JW3708
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11198. glmU.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141G → A: 8-fold decrease in uridyltransferase activity. Creates steric conflict and decreases affinity for UTP. 1 Publication
Mutagenesisi18 – 181R → A: Dramatically impairs the uridyltransferase activity. 1 Publication
Mutagenesisi25 – 251K → A: 8-fold decrease in uridyltransferase activity. 1 Publication
Mutagenesisi296 – 2961C → A: No effect. 1 Publication
Mutagenesisi307 – 3071C → A: 1350-fold decrease in acetyltransferase activity. 1 Publication
Mutagenesisi324 – 3241C → A: 8-fold decrease in acetyltransferase activity. 1 Publication
Mutagenesisi385 – 3851C → A: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Bifunctional protein GlmUUniRule annotationPRO_0000068701Add
BLAST

Proteomic databases

PaxDbiP0ACC7.
PRIDEiP0ACC7.

Expressioni

Gene expression databases

GenevestigatoriP0ACC7.

Interactioni

Subunit structurei

Homotrimer. In vivo forms a hexameric aggregate.4 Publications

Protein-protein interaction databases

DIPiDIP-31844N.
IntActiP0ACC7. 19 interactions.
MINTiMINT-1252604.
STRINGi511145.b3730.

Structurei

Secondary structure

1
456
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127
Helixi17 – 193
Helixi25 – 273
Beta strandi28 – 303
Helixi35 – 4612
Beta strandi51 – 555
Helixi59 – 657
Turni66 – 683
Beta strandi71 – 755
Helixi82 – 898
Helixi90 – 923
Beta strandi97 – 1037
Helixi111 – 12010
Beta strandi125 – 1328
Beta strandi141 – 1455
Beta strandi148 – 1536
Turni155 – 1573
Helixi162 – 1643
Beta strandi167 – 17610
Helixi177 – 1848
Beta strandi191 – 1933
Helixi198 – 2003
Helixi201 – 2066
Turni207 – 2093
Beta strandi212 – 2154
Helixi220 – 2234
Helixi233 – 24917
Beta strandi253 – 2553
Helixi257 – 2593
Beta strandi260 – 2689
Beta strandi278 – 2869
Beta strandi297 – 3004
Beta strandi314 – 3174
Beta strandi325 – 3273
Beta strandi328 – 3325
Beta strandi336 – 3383
Beta strandi343 – 35513
Beta strandi360 – 37213
Beta strandi383 – 3853
Beta strandi387 – 3904
Beta strandi395 – 3973
Beta strandi408 – 4158

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FWYX-ray2.30A/B1-331[»]
1FXJX-ray2.25A/B1-331[»]
1HV9X-ray2.10A/B1-456[»]
2OI5X-ray2.25A/B1-456[»]
2OI6X-ray2.20A/B1-456[»]
2OI7X-ray2.54A/B1-456[»]
3TWDX-ray1.90A/B233-452[»]
4AA7X-ray2.00A/B227-456[»]
ProteinModelPortaliP0ACC7.
SMRiP0ACC7. Positions 3-451.

Miscellaneous databases

EvolutionaryTraceiP0ACC7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 229229PyrophosphorylaseUniRule annotationAdd
BLAST
Regioni11 – 144UDP-GlcNAc bindingUniRule annotation
Regioni81 – 822UDP-GlcNAc bindingUniRule annotation
Regioni103 – 1053UDP-GlcNAc bindingUniRule annotation
Regioni230 – 25021LinkerUniRule annotationAdd
BLAST
Regioni251 – 456206N-acetyltransferaseUniRule annotationAdd
BLAST
Regioni386 – 3872Acetyl-CoA bindingUniRule annotation

Sequence similaritiesi

In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.
In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1207.
HOGENOMiHOG000283476.
KOiK04042.
OMAiDCVTNQD.
OrthoDBiEOG6Z6FQZ.
PhylomeDBiP0ACC7.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01173. glmU. 1 hit.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ACC7-1 [UniParc]FASTAAdd to Basket

« Hide

MLNNAMSVVI LAAGKGTRMY SDLPKVLHTL AGKAMVQHVI DAANELGAAH    50
VHLVYGHGGD LLKQALKDDN LNWVLQAEQL GTGHAMQQAA PFFADDEDIL 100
MLYGDVPLIS VETLQRLRDA KPQGGIGLLT VKLDDPTGYG RITRENGKVT 150
GIVEHKDATD EQRQIQEINT GILIANGADM KRWLAKLTNN NAQGEYYITD 200
IIALAYQEGR EIVAVHPQRL SEVEGVNNRL QLSRLERVYQ SEQAEKLLLA 250
GVMLRDPARF DLRGTLTHGR DVEIDTNVII EGNVTLGHRV KIGTGCVIKN 300
SVIGDDCEIS PYTVVEDANL AAACTIGPFA RLRPGAELLE GAHVGNFVEM 350
KKARLGKGSK AGHLTYLGDA EIGDNVNIGA GTITCNYDGA NKFKTIIGDD 400
VFVGSDTQLV APVTVGKGAT IAAGTTVTRN VGENALAISR VPQTQKEGWR 450
RPVKKK 456
Length:456
Mass (Da):49,190
Last modified:November 8, 2005 - v1
Checksum:i2F3C5C84F673C8A3
GO

Sequence cautioni

The sequence AAA62081.1 differs from that shown. Reason: Frameshift at position 179. Produces two ORFs.
The sequence AAA62082.1 differs from that shown. Reason: Frameshift at position 179. Produces two ORFs.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1872KL → NV in CAA25784. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
PIRiC65176.
RefSeqiNP_418186.1. NC_000913.3.
YP_491699.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76753; AAC76753; b3730.
BAE77558; BAE77558; BAE77558.
GeneIDi12933149.
948246.
KEGGiecj:Y75_p3438.
eco:b3730.
PATRICi32122957. VBIEscCol129921_3854.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_491699.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P0ACC7.
SMRi P0ACC7. Positions 3-451.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-31844N.
IntActi P0ACC7. 19 interactions.
MINTi MINT-1252604.
STRINGi 511145.b3730.

Proteomic databases

PaxDbi P0ACC7.
PRIDEi P0ACC7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76753 ; AAC76753 ; b3730 .
BAE77558 ; BAE77558 ; BAE77558 .
GeneIDi 12933149.
948246.
KEGGi ecj:Y75_p3438.
eco:b3730.
PATRICi 32122957. VBIEscCol129921_3854.

Organism-specific databases

EchoBASEi EB1184.
EcoGenei EG11198. glmU.

Phylogenomic databases

eggNOGi COG1207.
HOGENOMi HOG000283476.
KOi K04042.
OMAi DCVTNQD.
OrthoDBi EOG6Z6FQZ.
PhylomeDBi P0ACC7.

Enzyme and pathway databases

UniPathwayi UPA00113 ; UER00532 .
UPA00113 ; UER00533 .
UPA00973 .
BioCyci EcoCyc:NAG1P-URIDYLTRANS-MONOMER.
ECOL316407:JW3708-MONOMER.
MetaCyc:NAG1P-URIDYLTRANS-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0ACC7.
PROi P0ACC7.

Gene expression databases

Genevestigatori P0ACC7.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
HAMAPi MF_01631. GlmU.
InterProi IPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view ]
Pfami PF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view ]
SUPFAMi SSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsi TIGR01173. glmU. 1 hit.
PROSITEi PS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS."
    Walker J.E., Gay N.J., Saraste M., Eberle A.N.
    Biochem. J. 224:799-815(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  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.
  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, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  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.
  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.
  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, MUTAGENESIS OF GLY-14; ARG-18 AND LYS-25.
  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 AND COA, COFACTOR, SUBUNIT.
  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, SUBUNIT.
  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, ENZYME REGULATION, SUBUNIT.
  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, ENZYME REGULATION, SUBUNIT.

Entry informationi

Entry nameiGLMU_ECOLI
AccessioniPrimary (citable) accession number: P0ACC7
Secondary accession number(s): P17114, P76746, Q2M848
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: June 11, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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