GM4D_AGGAC
ID GM4D_AGGAC Reviewed; 344 AA.
AC Q9JRN5;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 75.
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};
OS Aggregatibacter actinomycetemcomitans (Actinobacillus
OS actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=714;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SUNYaB 75 / Serotype a;
RX PubMed=11118626; DOI=10.1016/s0167-4781(00)00229-3;
RA Suzuki N., Nakano Y., Yoshida Y., Nakao H., Yamashita Y., Koga T.;
RT "Genetic analysis of the gene cluster for the synthesis of serotype a-
RT specific polysaccharide antigen in Aactinobacillus actinomycetemcomitans.";
RL Biochim. Biophys. Acta 1517:135-138(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RC STRAIN=SUNYaB 75 / Serotype a;
RX PubMed=12444986; DOI=10.1046/j.1432-1033.2002.03331.x;
RA Suzuki N., Nakano Y., Yoshida Y., Nezu T., Terada Y., Yamashita Y.,
RA Koga T.;
RT "Guanosine diphosphate-4-keto-6-deoxy-d-mannose reductase in the pathway
RT for the synthesis of GDP-6-deoxy-d-talose in Actinobacillus
RT actinomycetemcomitans.";
RL Eur. J. Biochem. 269:5963-5971(2002).
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 ECO:0000269|PubMed:12444986}.
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, ECO:0000269|PubMed:12444986};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00955,
CC ECO:0000269|PubMed:12444986};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:12444986}.
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 {ECO:0000269|PubMed:12444986}.
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; AB046360; BAB03208.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9JRN5; -.
DR SMR; Q9JRN5; -.
DR STRING; 714.ACT75_06335; -.
DR eggNOG; COG1089; Bacteria.
DR BioCyc; MetaCyc:MON-13569; -.
DR UniPathway; UPA00128; UER00190.
DR UniPathway; UPA00281; -.
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 GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW Lipopolysaccharide biosynthesis; Lyase; NADP.
FT CHAIN 1..344
FT /note="GDP-mannose 4,6-dehydratase"
FT /id="PRO_0000424095"
FT ACT_SITE 127
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT ACT_SITE 129
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT ACT_SITE 151
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 8..13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 60..61
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 82..86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 181
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
FT BINDING 186
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00955"
SQ SEQUENCE 344 AA; 38986 MW; E62121713149B5F2 CRC64;
MKTAIVTGAS GQDGAYLSQL LLDKGYKVYA TYRRSSSVNL WRIDELNIRN HPNLHLFEFD
LTDMSSCISL VTKAQPGEVY NLAAQSFVGV SFSQPVTTAE ITAIGVLNLL EAIRIINPKI
KFYQASTSEM FGKVQQIPQT EKTPFYPRSP YGVAKLYGHW ITLNYRESYD IFGCSGILFN
HESPLRGREF VTRKITDTVA KIALNKQSCL ELGNLDAKRD WGFAKEYVEG MWRMLQEDQP
DTYVLATNRT ETVRDFVAMA FQAVNIPLEF NGKGENEIGV NTDTGDVLVR VNKEYYRPAE
VDLLIGDYSK AKRILGWEPK TSLEELCKMM IEADIERNKL GFSF
