ID A0A495AJK4_9ENTR Unreviewed; 376 AA.
AC A0A495AJK4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=UDP-N-acetylglucosamine 2-epimerase {ECO:0000256|HAMAP-Rule:MF_02028};
DE EC=5.1.3.14 {ECO:0000256|HAMAP-Rule:MF_02028};
DE AltName: Full=UDP-GlcNAc-2-epimerase {ECO:0000256|HAMAP-Rule:MF_02028};
GN Name=wecB {ECO:0000256|HAMAP-Rule:MF_02028};
GN ORFNames=D8M09_08165 {ECO:0000313|EMBL:RKQ40211.1};
OS Enterobacter sp. R1(2018).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=2447891 {ECO:0000313|EMBL:RKQ40211.1, ECO:0000313|Proteomes:UP000271976};
RN [1] {ECO:0000313|EMBL:RKQ40211.1, ECO:0000313|Proteomes:UP000271976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1(2018) {ECO:0000313|Proteomes:UP000271976};
RA Ontanon O.M., Ghio S., Rivarola M., Campos E.;
RT "Enterobacter sp. from a bacterial cellulose degrading consortium draft
RT genome.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible epimerization at C-2 of UDP-N-
CC acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP-
CC N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc
CC residues. {ECO:0000256|HAMAP-Rule:MF_02028}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-
CC mannosamine; Xref=Rhea:RHEA:17213, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:68623; EC=5.1.3.14;
CC Evidence={ECO:0000256|ARBA:ARBA00036080, ECO:0000256|HAMAP-
CC Rule:MF_02028};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02028}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02028}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02028}.
CC -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC {ECO:0000256|ARBA:ARBA00038209, ECO:0000256|HAMAP-Rule:MF_02028,
CC ECO:0000256|RuleBase:RU003513}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKQ40211.1}.
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DR EMBL; RCAA01000030; RKQ40211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495AJK4; -.
DR OrthoDB; 9803238at2; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000271976; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03786; GTB_UDP-GlcNAc_2-Epimerase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR HAMAP; MF_02028; WecB_RffE; 1.
DR InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR InterPro; IPR032892; WecB.
DR InterPro; IPR029767; WecB-like.
DR NCBIfam; TIGR00236; wecB; 1.
DR PANTHER; PTHR43174; UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE; 1.
DR PANTHER; PTHR43174:SF2; UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE; 1.
DR Pfam; PF02350; Epimerase_2; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02028};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_02028}.
FT DOMAIN 22..370
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02028"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02028"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02028"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02028"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02028"
FT BINDING 290..292
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02028"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02028"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02028"
SQ SEQUENCE 376 AA; 42034 MW; 5F91C72ECFBFF237 CRC64;
MKVLTVFGTR PEAIKMAPLV HALAKDAFFD AKVCVTAQHR EMLDQVLNLF SIKPDYDLNI
MSPGQGLTEI TCRILEGLKP ILETFKPDVV LVHGDTTTTV ATSLAAFYQR IPVGHVEAGL
RTGDLYTPWP EEANRTLTGH LAMYHFAPTE NSRQNLLREN ISDNKIFVTG NTVIDALISV
RDRVLADDEL RDSLARYHPF LDSAKKLILV TGHRRESFGN GFERICHALA EIARENSDVQ
IVYPVHLNPN VSEPVKRILG DVENVVLAEP QEYLPFVYLM NHAYLILTDS GGIQEEAPSL
GKPVLVMRDT TERPEAVKAG TVRLVGTDTQ TIVREVTRLL RDENEYQIMS RAHNPYGDGT
ACERILTALK NNQVKL
//
