GM4D_VIBCH
ID GM4D_VIBCH Reviewed; 373 AA.
AC Q06952;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
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;
GN OrderedLocusNames=VC_0243;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=El Tor O17 / Serotype O1;
RX PubMed=1372980; DOI=10.1073/pnas.89.7.2566;
RA Stroeher U.H., Karageorgos L.E., Morona R., Manning P.A.;
RT "Serotype conversion in Vibrio cholerae O1.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2566-2570(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=El Tor O17 / Serotype O1;
RX PubMed=7540582; DOI=10.1016/0378-1119(95)00124-o;
RA Manning P.A., Stroeher U.H., Karageorgos L.E., Morona R.;
RT "Putative O-antigen transport genes within the rfb region of Vibrio
RT cholerae O1 are homologous to those for capsule transport.";
RL Gene 158:1-7(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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 -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. GDP-mannose 4,6-dehydratase subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00955}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X59554; CAA42136.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF93419.1; -; Genomic_DNA.
DR PIR; S28470; S28470.
DR RefSeq; NP_229900.1; NC_002505.1.
DR RefSeq; WP_001036868.1; NZ_LT906614.1.
DR AlphaFoldDB; Q06952; -.
DR SMR; Q06952; -.
DR STRING; 243277.VC_0243; -.
DR DNASU; 2614706; -.
DR EnsemblBacteria; AAF93419; AAF93419; VC_0243.
DR GeneID; 57738979; -.
DR KEGG; vch:VC_0243; -.
DR PATRIC; fig|243277.26.peg.224; -.
DR eggNOG; COG1089; Bacteria.
DR HOGENOM; CLU_007383_14_0_6; -.
DR OMA; TDCLYLG; -.
DR BioCyc; MetaCyc:MON-13574; -.
DR BioCyc; VCHO:VC0243-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IBA:GO_Central.
DR GO; GO:0070401; F:NADP+ binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IBA:GO_Central.
DR GO; GO:0019673; P:GDP-mannose metabolic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..373
FT /note="GDP-mannose 4,6-dehydratase"
FT /id="PRO_0000201717"
FT ACT_SITE 134
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT ACT_SITE 136
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT ACT_SITE 158
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 10..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 65..66
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 87..91
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 102
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 162
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 188
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
SQ SEQUENCE 373 AA; 42053 MW; 4EB10DCAB6A8C1D2 CRC64;
MNKKVALITG ITGQDGSYLA EFLLEKGYEV HGIKRRSSLF NTQRVDHLYK DPHEEDVNFK
LHYGDLTDSS NLTRILAEVQ PDEVYNLGAQ SHVAVSFQSP EYTADVDAIG TLRLLEAIRF
LGLTKKTKFY QASTSELYGL VQEIPQKETT PFYPRSPYAV AKMYAYWITI NYRESYGIYA
CNGILFNHES PRRGETFVTR KITRGMANIA QGLEKCLFMG NLDALRDWGH AKDYVKMQWM
MLQQDEPRDF VIATGVQYSV REFIDMSARE LGIELEFVGK GVDEKAVVKS VIGTKAPAIK
VGDIIVAVDP AYFRPAEVET LLGDPSLAKK ELGWVPEITL QQMVSEMVAS DLEQAQSHAL
LKKHGYNVNV SVE
