GM4D_RHIFH
ID GM4D_RHIFH Reviewed; 351 AA.
AC O85713; G9ACH2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=noeL;
GN OrderedLocusNames=SFHH103_04266;
OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii).
OG Plasmid pSfHH103d.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=1117943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HH103;
RX PubMed=10065558; DOI=10.1094/mpmi.1999.12.3.207;
RA Lamrabet Y., Bellogin R.A., Cubo T., Espuny R., Gil A., Krishnan H.B.,
RA Megias M., Ollero F.J., Pueppke S.G., Ruiz-Sainz J.E., Spaink H.P.,
RA Tejero-Mateo P., Thomas-Oates J., Vinardell J.M.;
RT "Mutation in GDP-fucose synthesis genes of Sinorhizobium fredii alters Nod
RT factors and significantly decreases competitiveness to nodulate soybeans.";
RL Mol. Plant Microbe Interact. 12:207-217(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH103;
RX PubMed=22374952; DOI=10.1128/jb.06729-11;
RA Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., Margaret I.,
RA Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., Szczepanowski R.,
RA Vinardell J.M., Zehner S., Gottfert M.;
RT "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103.";
RL J. Bacteriol. 194:1617-1618(2012).
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; AF072888; AAC27750.1; -; Genomic_DNA.
DR EMBL; HE616895; CCE98752.1; -; Genomic_DNA.
DR RefSeq; WP_014857595.1; NT_187147.1.
DR AlphaFoldDB; O85713; -.
DR SMR; O85713; -.
DR GeneID; 48977684; -.
DR HOGENOM; CLU_007383_14_0_5; -.
DR OMA; FVKSSWQ; -.
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; Nodulation; Plasmid.
FT CHAIN 1..351
FT /note="GDP-mannose 4,6-dehydratase"
FT /id="PRO_0000201720"
FT ACT_SITE 135
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT ACT_SITE 137
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT ACT_SITE 159
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 11..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 66..67
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 88..92
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 103
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 163
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 194
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
SQ SEQUENCE 351 AA; 40014 MW; 0E6A32874B3061EB CRC64;
MTDRKVALIS GVTGQDGAYL AELLLDEGYI VHGIKRRSSS FNTQRIEHIY QERHDPEARF
FLHYGDMTDS TNLLRIVQQT QPHEIYNLAA QSHVQVSFET PEYTANADAI GTLRMLEAIR
ILGLIHRTRF YQASTSELYG LAQEIPQNEK TPFYPRSPYA AAKLYAYWIV VNYREAYGMH
ASNGILFNHE SPLRGETFVT RKITRAAAAI SLGKQEVLYL GNLDAQRDWG HAREYVRGMW
MMCQQDRPGD YVLATGVTTS VRTFVEWAFE ETGMTIEWVG EGIEERGIDA ATGKCVVAVD
PRYFRPTEVD LLLGDATKAR QVLGWRHETS VRDLACEMVR EDLSYLRGTR Q
