ID Q0AZ05_SYNWW Unreviewed; 337 AA.
AC Q0AZ05;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=UDP-glucose 4-epimerase {ECO:0000256|ARBA:ARBA00018569};
DE EC=5.1.3.2 {ECO:0000256|ARBA:ARBA00013189};
DE AltName: Full=Galactowaldenase {ECO:0000256|ARBA:ARBA00033067};
DE AltName: Full=UDP-galactose 4-epimerase {ECO:0000256|ARBA:ARBA00031367};
GN OrderedLocusNames=Swol_0726 {ECO:0000313|EMBL:ABI68049.1};
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI68049.1, ECO:0000313|Proteomes:UP000001968};
RN [1] {ECO:0000313|Proteomes:UP000001968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968};
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI68049.1; -; Genomic_DNA.
DR RefSeq; WP_011640154.1; NC_008346.1.
DR AlphaFoldDB; Q0AZ05; -.
DR STRING; 335541.Swol_0726; -.
DR KEGG; swo:Swol_0726; -.
DR eggNOG; COG1086; Bacteria.
DR HOGENOM; CLU_013560_4_1_9; -.
DR OMA; HEVMIPK; -.
DR OrthoDB; 9803111at2; -.
DR Proteomes; UP000001968; Chromosome.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:InterPro.
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:UP000001968}.
FT DOMAIN 8..281
FT /note="Polysaccharide biosynthesis protein CapD-like"
FT /evidence="ECO:0000259|Pfam:PF02719"
FT DOMAIN 284..331
FT /note="UDP-glucose 4-epimerase CapD C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08485"
SQ SEQUENCE 337 AA; 38341 MW; 5F2FA64110BC78C5 CRC64;
MFNGTTLIIT GGTGTFGNAV LKRFLDTDIR EIRIFSRDEK KQYDMRTQLM NHKIKFYIGD
VRNYESIESA MYGVDYVFHA AALKQVPSCE FYPMEAVRTN ILGTENVLNA AIKNHVRKMI
VLGTDKAVYP INAMGISKAM MEKVMVAKAR TMDEKGTVFC GTRYGNVMAS RGSVIPLFVD
QIKSGQALTV TDPNMTRFLM SIEDAVDLVL YAYEHGSQGD IFVQKAPAAT IGDLALALKE
LFNADNEIKI IGTRHGEKLY ETLLTREELV RAEDLGRYYR VPADQRDLNY NKYFIEGQEQ
LSYQEDYHSH NTRRLNVSEI KEMLLTLDYI KQQLGSR
//