ID A0A1H4FSY3_9GAMM Unreviewed; 376 AA.
AC A0A1H4FSY3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN02982996_03222 {ECO:0000313|EMBL:SEB00394.1};
OS Lonsdalea quercina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Lonsdalea.
OX NCBI_TaxID=71657 {ECO:0000313|EMBL:SEB00394.1, ECO:0000313|Proteomes:UP000187280};
RN [1] {ECO:0000313|EMBL:SEB00394.1, ECO:0000313|Proteomes:UP000187280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29281 {ECO:0000313|EMBL:SEB00394.1,
RC ECO:0000313|Proteomes:UP000187280};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNQS01000015; SEB00394.1; -; Genomic_DNA.
DR RefSeq; WP_074729376.1; NZ_FNQS01000015.1.
DR AlphaFoldDB; A0A1H4FSY3; -.
DR STRING; 71657.SAMN02982996_03222; -.
DR eggNOG; COG0381; Bacteria.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000187280; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000187280}.
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; 41840 MW; 4D8363BBA11A75CE CRC64;
MKVLTVFGTR PEAIKMAPLI HALAQDTFFE SRICVTAQHR EMLDQVLELF GIEPDFDLNI
MQPGQGLSEI SCRILSGLKP VLEAFRPDLV LVHGDTSTTL MASLAAFYQR IPVGHVEAGL
RTGDIYAPWP EEANRTLTGH LAQFHFAPTD SARLNLLKEN VPDAAINVTG NTVIDALYWV
RDLIARDPKL NRPLQAQYAF LSEQRKMILV TGHRRESFGN GFERICHALA EIAHRHPDVQ
IVYPVHLNPN VSEPVNRILS GIDNIFLIAP QNYLPFVYLM NRAYLILTDS GGIQEEAPSL
GKPVLVMRDT TERPEALASG VVRLVGTDTT KILHNVSELL TDESAYRAMS QAQNPYGDGH
ASQRILAALK ENQVRL
//
