ID A0A3T0NAQ2_9RHOB Unreviewed; 373 AA.
AC A0A3T0NAQ2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=GDP-mannose 4,6-dehydratase {ECO:0000256|ARBA:ARBA00011989, ECO:0000256|HAMAP-Rule:MF_00955};
DE EC=4.2.1.47 {ECO:0000256|ARBA:ARBA00011989, ECO:0000256|HAMAP-Rule:MF_00955};
DE AltName: Full=GDP-D-mannose dehydratase {ECO:0000256|HAMAP-Rule:MF_00955};
GN Name=gmd {ECO:0000256|HAMAP-Rule:MF_00955,
GN ECO:0000313|EMBL:AZV81052.1};
GN ORFNames=EBB79_24545 {ECO:0000313|EMBL:AZV81052.1};
OS Parasedimentitalea marina.
OG Plasmid pw43d {ECO:0000313|Proteomes:UP000283063}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Parasedimentitalea.
OX NCBI_TaxID=2483033 {ECO:0000313|EMBL:AZV81052.1, ECO:0000313|Proteomes:UP000283063};
RN [1] {ECO:0000313|EMBL:AZV81052.1, ECO:0000313|Proteomes:UP000283063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W43 {ECO:0000313|EMBL:AZV81052.1,
RC ECO:0000313|Proteomes:UP000283063};
RC PLASMID=pw43d {ECO:0000313|Proteomes:UP000283063};
RA Cao J.;
RT "Parasedimentitalea marina sp. nov., a psychrophilic bacterium isolated
RT from deep seawater of the New Britain Trench.";
RL Submitted (OCT-2018) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_00955};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000256|ARBA:ARBA00001937,
CC ECO:0000256|HAMAP-Rule:MF_00955};
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. GDP-mannose 4,6-dehydratase subfamily.
CC {ECO:0000256|ARBA:ARBA00009263, ECO:0000256|HAMAP-Rule:MF_00955}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00955}.
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DR EMBL; CP033223; AZV81052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3T0NAQ2; -.
DR KEGG; sedi:EBB79_24545; -.
DR OrthoDB; 9779041at2; -.
DR Proteomes; UP000283063; Plasmid pw43d.
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:0019673; P:GDP-mannose metabolic process; IEA:InterPro.
DR CDD; cd05260; GDP_MD_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
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 NCBIfam; TIGR01472; gmd; 1.
DR PANTHER; PTHR43715:SF1; GDP-MANNOSE 4,6 DEHYDRATASE; 1.
DR PANTHER; PTHR43715; GDP-MANNOSE 4,6-DEHYDRATASE; 1.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00955, ECO:0000313|EMBL:AZV81052.1};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00955};
KW Plasmid {ECO:0000313|EMBL:AZV81052.1}.
FT DOMAIN 6..346
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 373 AA; 41944 MW; 5F9FBD5F02FAEBD7 CRC64;
MSKIALITGV TGQDGSYLAE FLLEKGYEVH GIKRRASSFN TQRVDHIYQD PHIDHAKFKL
HYGDLSDSSN LTRILKEVQP DEVYNLGAQS HVAVSFDAPE YTADVDAMGT LRLLEAIRFL
GLEKKTRFYQ ASTSELYGLV QETPQTETTP FHPRSPYAVA KMYAYWITVN YREAYGMYAC
NGILFNHESP RRGETFVTRK ITRGLANMAQ GLEPCLYMGN IDSLRDWGHA KDYVRMQWMM
LQQDAPDDFV IATGVQYSVR DFINWSAAEL GITLDFSGSG VDEIATVSAI SGDEAPGLSV
GDVILRIDPR YFRPAEVETL LGDPTKAKEK LGWVPETTVQ EMCAEMVRED LKAAKRARVL
KDHGYDLPVT RGE
//
