We will be switching to the new UniProt website soon. Please explore and share your feedback.
Take me to the new website.
UniProtKB - P27828 (WECB_ECOLI)
Protein
UDP-N-acetylglucosamine 2-epimerase
Gene
wecB
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the reversible epimerization at C-2 of UDP-N-acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP-N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc residues. Also involved in bacteriophage N4 adsorption.
5 PublicationsCatalytic activityi
- EC:5.1.3.14UniRule annotation2 Publications
Activity regulationi
Allosterically activated by its substrate, UDP-GlcNAc.1 Publication
Kineticsi
kcat is 7.1 sec(-1).1 Publication
- KM=0.6 mM for UDP-GlcNAc1 Publication
: enterobacterial common antigen biosynthesis Pathwayi
This protein is involved in the pathway enterobacterial common antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotation1 PublicationView all proteins of this organism that are known to be involved in the pathway enterobacterial common antigen biosynthesis and in Bacterial outer membrane biogenesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 10 | SubstrateUniRule annotation2 Publications | 1 | |
Binding sitei | 15 | SubstrateUniRule annotation1 Publication | 1 | |
Binding sitei | 95 | SubstrateUniRule annotation1 Publication | 1 | |
Binding sitei | 117 | SubstrateUniRule annotation1 Publication | 1 | |
Binding sitei | 213 | SubstrateUniRule annotation2 Publications | 1 | |
Binding sitei | 271 | Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation2 Publications | 1 | |
Binding sitei | 276 | SubstrateUniRule annotation2 Publications | 1 | |
Binding sitei | 296 | SubstrateUniRule annotation2 Publications | 1 | |
Binding sitei | 313 | SubstrateUniRule annotation1 Publication | 1 |
GO - Molecular functioni
- identical protein binding Source: EcoCyc
- UDP-N-acetylglucosamine 2-epimerase activity Source: EcoCyc
GO - Biological processi
- enterobacterial common antigen biosynthetic process Source: EcoCyc
Keywordsi
Molecular function | Allosteric enzyme, Isomerase |
Enzyme and pathway databases
BioCyci | EcoCyc:UDPGLCNACEPIM-MONOMER |
BRENDAi | 3.2.1.183, 1960 5.1.3.14, 2026 |
SABIO-RKi | P27828 |
UniPathwayi | UPA00566 |
Names & Taxonomyi
Protein namesi | Recommended name: UDP-N-acetylglucosamine 2-epimeraseUniRule annotationCurated (EC:5.1.3.14UniRule annotation2 Publications)Alternative name(s): Bacteriophage N4 adsorption protein C1 Publication UDP-GlcNAc-2-epimeraseUniRule annotationCurated |
Gene namesi | Name:wecBUniRule annotation Synonyms:nfrC1 Publication, rffE1 Publication, yifF Ordered Locus Names:b3786, JW5600 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation1 Publication
Cytosol
- cytosol Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 15 | K → A: More than 100-fold increase in KM for UDP-GlcNAc. 1 Publication | 1 | |
Mutagenesisi | 95 | D → N: Strong decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 117 | E → Q: Strong decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 131 | E → Q: Strong decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 213 | H → N: 30-fold increase in KM for UDP-GlcNAc and 50-fold decrease in kcat. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB03435, Uridine-5'-Diphosphate DB02196, Uridine-Diphosphate-N-Acetylgalactosamine |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000208527 | 1 – 376 | UDP-N-acetylglucosamine 2-epimeraseAdd BLAST | 376 |
Proteomic databases
jPOSTi | P27828 |
PaxDbi | P27828 |
PRIDEi | P27828 |
Interactioni
Subunit structurei
Homodimer.
UniRule annotation1 PublicationGO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4263321, 147 interactors |
STRINGi | 511145.b3786 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P27828 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P27828 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 290 – 292 | Substrate bindingUniRule annotation2 Publications | 3 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0381, Bacteria |
HOGENOMi | CLU_041674_1_0_6 |
InParanoidi | P27828 |
PhylomeDBi | P27828 |
Family and domain databases
HAMAPi | MF_02028, WecB_RffE, 1 hit |
InterProi | View protein in InterPro IPR003331, UDP_GlcNAc_Epimerase_2_dom IPR032892, WecB IPR029767, WecB-like |
PANTHERi | PTHR43174, PTHR43174, 1 hit |
Pfami | View protein in Pfam PF02350, Epimerase_2, 1 hit |
TIGRFAMsi | TIGR00236, wecB, 1 hit |
i Sequence
Sequence statusi: Complete.
P27828-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKVLTVFGTR PEAIKMAPLV HALAKDPFFE AKVCVTAQHR EMLDQVLKLF
60 70 80 90 100
SIVPDYDLNI MQPGQGLTEI TCRILEGLKP ILAEFKPDVV LVHGDTTTTL
110 120 130 140 150
ATSLAAFYQR IPVGHVEAGL RTGDLYSPWP EEANRTLTGH LAMYHFSPTE
160 170 180 190 200
TSRQNLLREN VADSRIFITG NTVIDALLWV RDQVMSSDKL RSELAANYPF
210 220 230 240 250
IDPDKKMILV TGHRRESFGR GFEEICHALA DIATTHQDIQ IVYPVHLNPN
260 270 280 290 300
VREPVNRILG HVKNVILIDP QEYLPFVWLM NHAWLILTDS GGIQEEAPSL
310 320 330 340 350
GKPVLVMRDT TERPEAVTAG TVRLVGTDKQ RIVEEVTRLL KDENEYQAMS
360 370
RAHNPYGDGQ ACSRILEALK NNRISL
Sequence cautioni
The sequence AAA67586 differs from that shown. Reason: Erroneous initiation.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 191 | Missing in AAA67586 (PubMed:1379743).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L18799 Unassigned DNA Translation: AAC36847.1 M87049 Genomic DNA Translation: AAA67586.1 Different initiation. U00096 Genomic DNA Translation: AAT48211.1 AP009048 Genomic DNA Translation: BAE77512.1 |
PIRi | E65182 |
RefSeqi | WP_001340422.1, NZ_SSZK01000025.1 YP_026253.1, NC_000913.3 |
Genome annotation databases
EnsemblBacteriai | AAT48211; AAT48211; b3786 BAE77512; BAE77512; BAE77512 |
GeneIDi | 944789 |
KEGGi | ecj:JW5600 eco:b3786 |
PATRICi | fig|511145.12.peg.3902 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L18799 Unassigned DNA Translation: AAC36847.1 M87049 Genomic DNA Translation: AAA67586.1 Different initiation. U00096 Genomic DNA Translation: AAT48211.1 AP009048 Genomic DNA Translation: BAE77512.1 |
PIRi | E65182 |
RefSeqi | WP_001340422.1, NZ_SSZK01000025.1 YP_026253.1, NC_000913.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1F6D | X-ray | 2.50 | A/B/C/D | 1-376 | [»] | |
1VGV | X-ray | 2.31 | A/B/C/D | 2-376 | [»] | |
SMRi | P27828 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263321, 147 interactors |
STRINGi | 511145.b3786 |
Chemistry databases
DrugBanki | DB03435, Uridine-5'-Diphosphate DB02196, Uridine-Diphosphate-N-Acetylgalactosamine |
Proteomic databases
jPOSTi | P27828 |
PaxDbi | P27828 |
PRIDEi | P27828 |
Genome annotation databases
EnsemblBacteriai | AAT48211; AAT48211; b3786 BAE77512; BAE77512; BAE77512 |
GeneIDi | 944789 |
KEGGi | ecj:JW5600 eco:b3786 |
PATRICi | fig|511145.12.peg.3902 |
Organism-specific databases
EchoBASEi | EB1420 |
Phylogenomic databases
eggNOGi | COG0381, Bacteria |
HOGENOMi | CLU_041674_1_0_6 |
InParanoidi | P27828 |
PhylomeDBi | P27828 |
Enzyme and pathway databases
UniPathwayi | UPA00566 |
BioCyci | EcoCyc:UDPGLCNACEPIM-MONOMER |
BRENDAi | 3.2.1.183, 1960 5.1.3.14, 2026 |
SABIO-RKi | P27828 |
Miscellaneous databases
EvolutionaryTracei | P27828 |
PROi | PR:P27828 |
Family and domain databases
HAMAPi | MF_02028, WecB_RffE, 1 hit |
InterProi | View protein in InterPro IPR003331, UDP_GlcNAc_Epimerase_2_dom IPR032892, WecB IPR029767, WecB-like |
PANTHERi | PTHR43174, PTHR43174, 1 hit |
Pfami | View protein in Pfam PF02350, Epimerase_2, 1 hit |
TIGRFAMsi | TIGR00236, wecB, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | WECB_ECOLI | |
Accessioni | P27828Primary (citable) accession number: P27828 Secondary accession number(s): P76753, Q2M894 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1992 |
Last sequence update: | July 1, 1993 | |
Last modified: | February 23, 2022 | |
This is version 160 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
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