COLC_YERPU
ID COLC_YERPU Reviewed; 308 AA.
AC G4WJD3;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=GDP-L-colitose synthase {ECO:0000303|PubMed:15610039};
DE EC=1.1.1.356 {ECO:0000269|PubMed:15610039};
GN Name=colC {ECO:0000303|PubMed:15610039}; Synonyms=colB, fcl;
OS Yersinia pseudotuberculosis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=633;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H720/86;
RX PubMed=21325338; DOI=10.1093/glycob/cwr010;
RA Cunneen M.M., Pacinelli E., Song W.C., Reeves P.R.;
RT "Genetic analysis of the O-antigen gene clusters of Yersinia
RT pseudotuberculosis O:6 and O:7.";
RL Glycobiology 21:1140-1146(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, SUBUNIT, PATHWAY, AND REACTION MECHANISM.
RX PubMed=15610039; DOI=10.1021/bi0483763;
RA Alam J., Beyer N., Liu H.W.;
RT "Biosynthesis of colitose: expression, purification, and mechanistic
RT characterization of GDP-4-keto-6-deoxy-D-mannose-3-dehydrase (ColD) and
RT GDP-L-colitose synthase (ColC).";
RL Biochemistry 43:16450-16460(2004).
CC -!- FUNCTION: Involved in the biosynthesis of the L-colitose (3,6-dideoxyl-
CC L-xylo-hexose) present in the O-antigen region of lipopolysaccharides
CC (LPS) where it serves as antigenic determinant and are vital for
CC bacterial defense and survival. Catalyzes the two-step NADP-dependent
CC conversion of GDP-4-keto-3,6-dideoxy-D-mannose to GDP-L-colitose. ColC
CC is a bifunctional enzyme catalyzing the C-5 epimerization of GDP-4-
CC keto-3,6-dideoxy-D-mannose and the subsequent C-4 keto reduction of the
CC resulting L-epimer to give GDP-L-colitose. It can use both NADP(+) and
CC NAD(+) as electron acceptor, with a slight preference for NADP(+).
CC {ECO:0000269|PubMed:15610039}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-colitose + NAD(+) = GDP-4-dehydro-3,6-dideoxy-
CC alpha-D-mannose + H(+) + NADH; Xref=Rhea:RHEA:36567,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:73931, ChEBI:CHEBI:73932; EC=1.1.1.356;
CC Evidence={ECO:0000269|PubMed:15610039};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-colitose + NADP(+) = GDP-4-dehydro-3,6-dideoxy-
CC alpha-D-mannose + H(+) + NADPH; Xref=Rhea:RHEA:36563,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:73931, ChEBI:CHEBI:73932; EC=1.1.1.356;
CC Evidence={ECO:0000269|PubMed:15610039};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=75 uM for GDP-4-keto-3,6-dideoxy-D-mannose (with NADP at pH 7.5
CC and 37 degrees Celsius) {ECO:0000269|PubMed:15610039};
CC KM=139 uM for GDP-4-keto-3,6-dideoxy-D-mannose (with NAD at pH 7.5
CC and 37 degrees Celsius) {ECO:0000269|PubMed:15610039};
CC Vmax=0.037 umol/min/mg enzyme toward GDP-4-keto-3,6-dideoxy-D-mannose
CC (with NADP at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:15610039};
CC Vmax=0.015 umol/min/mg enzyme toward GDP-4-keto-3,6-dideoxy-D-mannose
CC (with NAD at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:15610039};
CC -!- PATHWAY: Nucleotide-sugar metabolism; GDP-L-colitose biosynthesis.
CC {ECO:0000305|PubMed:15610039}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15610039}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Fucose synthase subfamily. {ECO:0000305}.
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DR EMBL; HQ456392; AEP25495.1; -; Genomic_DNA.
DR AlphaFoldDB; G4WJD3; -.
DR SMR; G4WJD3; -.
DR KEGG; ag:AEP25495; -.
DR UniPathway; UPA01070; -.
DR GO; GO:0050577; F:GDP-L-fucose synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0070401; F:NADP+ binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd05239; GDP_FS_SDR_e; 1.
DR HAMAP; MF_00956; GDP_fucose_synth; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR028614; GDP_fucose/colitose_synth.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Isomerase; NAD; NADP; Oxidoreductase.
FT CHAIN 1..308
FT /note="GDP-L-colitose synthase"
FT /id="PRO_0000435689"
FT ACT_SITE 132
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT BINDING 7..13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT BINDING 101..104
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT BINDING 136
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT BINDING 160..163
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT BINDING 176
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT SITE 103
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT SITE 105
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
SQ SEQUENCE 308 AA; 34768 MW; E4B53BB5F487D54E CRC64;
MKILLTGAGG MVGKNILAHT KSKDYEFITP SSKELDLLEK KHITTYLKHH KPNFIIHAAG
IVGGIHANIN NPVKFLVENM QMGINLLTAA KDNNIRKLLN LGSSCMYPKD CDSGLTEDMI
LTGELESTNE GYALAKITSA KLCEYINRED SEFQYKTAIP CNLYGKYDKF DENNSHMIPA
VIKKIVTAIE TGKSEVEIWG DGEARREFMY AEDLADFIFY TINNFTKMPQ NINVGLGQDY
TITEYYKVIA KILGYKGTFV YDKSKPVGMR RKLIDNTLLS EFGWSNKVDL ESGISKTCQY
FLNEKNND
