ID   GM4D_VIBCL              Reviewed;         372 AA.
AC   Q56598;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=GDP-mannose 4,6-dehydratase {ECO:0000255|HAMAP-Rule:MF_00955};
DE            EC=4.2.1.47 {ECO:0000255|HAMAP-Rule:MF_00955};
DE   AltName: Full=GDP-D-mannose dehydratase {ECO:0000255|HAMAP-Rule:MF_00955};
GN   Name=gmd {ECO:0000255|HAMAP-Rule:MF_00955}; Synonyms=rfbD;
OS   Vibrio cholerae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AI-1837 / Serotype O139;
RX   PubMed=9098074; DOI=10.1128/jb.179.8.2740-2747.1997;
RA   Stroeher U.H., Parasivam G., Dredge B.K., Manning P.A.;
RT   "Novel Vibrio cholerae O139 genes involved in lipopolysaccharide
RT   biosynthesis.";
RL   J. Bacteriol. 179:2740-2747(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51394 / MO45 / Serotype O139;
RX   PubMed=10521656; DOI=10.1016/s0378-1119(99)00344-3;
RA   Yamasaki S., Shimizu T., Hoshino K., Ho S.-T., Shimada T., Nair G.B.,
RA   Takeda Y.;
RT   "The genes responsible for O-antigen synthesis of Vibrio cholerae O139 are
RT   closely related to those of Vibrio cholerae O22.";
RL   Gene 237:321-332(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-348.
RC   STRAIN=ATCC 51394 / MO45 / Serotype O139;
RA   Dumontier S.E., Escuyer V.E., Berche P.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-
CC       deoxy-D-mannose. {ECO:0000255|HAMAP-Rule:MF_00955}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O;
CC         Xref=Rhea:RHEA:23820, ChEBI:CHEBI:15377, ChEBI:CHEBI:57527,
CC         ChEBI:CHEBI:57964; EC=4.2.1.47; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00955};
CC   -!- COFACTOR:
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00955};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via
CC       de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 1/2.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. GDP-mannose 4,6-dehydratase subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00955}.
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DR   EMBL; Y07786; CAA69111.1; -; Genomic_DNA.
DR   EMBL; AB012956; BAA33595.1; -; Genomic_DNA.
DR   EMBL; U24571; AAA77032.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q56598; -.
DR   SMR; Q56598; -.
DR   PATRIC; fig|666.1969.peg.2989; -.
DR   UniPathway; UPA00128; UER00190.
DR   GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070401; F:NADP+ binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019673; P:GDP-mannose metabolic process; IEA:InterPro.
DR   HAMAP; MF_00955; GDP_Man_dehydratase; 1.
DR   InterPro; IPR006368; GDP_Man_deHydtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43715; PTHR43715; 1.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01472; gmd; 1.
PE   3: Inferred from homology;
KW   Lyase; NADP.
FT   CHAIN           1..372
FT                   /note="GDP-mannose 4,6-dehydratase"
FT                   /id="PRO_0000201718"
FT   ACT_SITE        133
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT   ACT_SITE        135
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT   ACT_SITE        157
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT   BINDING         9..14
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT   BINDING         64..65
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT   BINDING         86..90
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT   BINDING         101
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT   BINDING         161
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT   BINDING         187
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT   BINDING         192
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
SQ   SEQUENCE   372 AA;  41992 MW;  11762663764B3E57 CRC64;
     MKKKALITGV TGQDGSYLAE FLLAKGYEVH GIKRRASSFN TQRVDHIYQD PHVDNASFIL
     HYGDLTDSSN LTRILQEVKP DEVYNLGAQS HVAVSFESPE YTADVDAMGT LRLLEAIRLL
     GLEKTTKFYQ ASTSELYGLV QETPQKETTP FYPRSPYAVA KMYAYWIVVN YRESYGMYAC
     NGILFNHESP RRGETFVTRK ITRGLANIAQ GLEKCLYMGN MDALRDWGHA KDYVRMQWMM
     LQQDQPEDFV IATGVQYSVR QFIEWSAKEL GVTLTFEGQG VDEKGIVTAI EGDKAPALKV
     GDVVVQIDPR YFRPAEVETL LGDPSKAKQK LGWTPEITVQ EMCAEMVMED LKVAQRHALL
     KLHGHDVPVS VE