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Database: UniProt
Entry: Q9CM37_PASMU
LinkDB: Q9CM37_PASMU
Original site: Q9CM37_PASMU 
ID   Q9CM37_PASMU            Unreviewed;       344 AA.
AC   Q9CM37;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=UDP-glucose 4-epimerase {ECO:0000256|ARBA:ARBA00018569};
DE            EC=5.1.3.2 {ECO:0000256|ARBA:ARBA00013189};
DE   AltName: Full=UDP-galactose 4-epimerase {ECO:0000256|ARBA:ARBA00031367};
GN   Name=wbjB {ECO:0000313|EMBL:AAK03091.1};
GN   OrderedLocusNames=PM1007 {ECO:0000313|EMBL:AAK03091.1};
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843 {ECO:0000313|EMBL:AAK03091.1, ECO:0000313|Proteomes:UP000000809};
RN   [1] {ECO:0000313|EMBL:AAK03091.1, ECO:0000313|Proteomes:UP000000809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70 {ECO:0000313|EMBL:AAK03091.1,
RC   ECO:0000313|Proteomes:UP000000809};
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose;
CC         Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914;
CC         EC=5.1.3.2; Evidence={ECO:0000256|ARBA:ARBA00000083};
CC   -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC       {ECO:0000256|ARBA:ARBA00007430}.
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DR   EMBL; AE004439; AAK03091.1; -; Genomic_DNA.
DR   RefSeq; WP_005723086.1; NC_002663.1.
DR   AlphaFoldDB; Q9CM37; -.
DR   STRING; 272843.PM1007; -.
DR   EnsemblBacteria; AAK03091; AAK03091; PM1007.
DR   KEGG; pmu:PM1007; -.
DR   HOGENOM; CLU_013560_4_1_6; -.
DR   OrthoDB; 9803111at2; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
DR   CDD; cd05237; UDP_invert_4-6DH_SDR_e; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013692; CapD_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003869; Polysac_CapD-like.
DR   PANTHER; PTHR43318; UDP-N-ACETYLGLUCOSAMINE 4,6-DEHYDRATASE; 1.
DR   PANTHER; PTHR43318:SF2; UDP-N-ACETYLGLUCOSAMINE 4,6-DEHYDRATASE (INVERTING); 1.
DR   Pfam; PF08485; Polysacc_syn_2C; 1.
DR   Pfam; PF02719; Polysacc_synt_2; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000809}.
FT   DOMAIN          7..282
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
FT   DOMAIN          285..332
FT                   /note="UDP-glucose 4-epimerase CapD C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08485"
SQ   SEQUENCE   344 AA;  38760 MW;  4B228313E07930C6 CRC64;
     MFKNKTLLIT GGTGSFGNAV LKRFLETDIR EIRVFSRDEK KQDDMRKKYN DAKLKFYIGD
     VRDYDSILNA SRGVDYIYHA AALKQVPSCE FYPLEAVKTN ILGTANVLEA AIQNQIKRVV
     CLSTDKAVYP INAMGISKAM MEKVIIAKSR NLEGTPTTIC CTRYGNVMAS RGSVIPLFVD
     QIRQGKPFTI TDPEMTRFMM TLEDAVDLVL YAFKNGQNGD VFVQKAPAAT IGTLAKAITE
     LLSVPNHPIS IIGTRHGEKA FEALLSREEM VHAINEGNYY RIPADQRSLN YSKYVEKGEP
     KITEVTDYNS HNTERLTVKE MKQLLLKLEF IQKMIEGEYI SPEV
//
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