ID A0A0G1IT02_9BACT Unreviewed; 325 AA.
AC A0A0G1IT02;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 ORFNames=UW24_C0018G0015 {ECO:0000313|EMBL:KKT34942.1};
OS Parcubacteria group bacterium GW2011_GWA2_44_12.
OC Bacteria.
OX NCBI_TaxID=1618829 {ECO:0000313|EMBL:KKT34942.1, ECO:0000313|Proteomes:UP000034439};
RN [1] {ECO:0000313|EMBL:KKT34942.1, ECO:0000313|Proteomes:UP000034439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKT34942.1}.
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DR EMBL; LCHO01000018; KKT34942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1IT02; -.
DR PATRIC; fig|1618829.3.peg.611; -.
DR Proteomes; UP000034439; Unassembled WGS sequence.
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 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};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00955}.
FT DOMAIN 6..314
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 325 AA; 37014 MW; 3A2D98003659EB15 CRC64;
MKKTALITGI LGQDGAYLAQ FLLSKEYKIF GMIRRHPFQN FVNTDYLGVT KEIEFISGDM
ADEASLMNIV RAVRPDEVYN LAAQSFVEDS WEQARLTTEV NALGVLYLLN AIKFFHPVAK
FYQASTSEMF GNSSGMNATN EHTPFYPRSP YGISKLYAHW MTINFRESYG MFCASGILFN
HESPLRGEEF VTRKIAKGAA EVKHGLQNAI SLGNLESKRD WGFAGDFVEA MWLMLQQEKA
KDYVIATGET HSVANFLESA FMYVGIKEWR NYVTVDPRFM RPAEVHYLRG DASYAKQKLG
WQPKVDFQAL VKLMVDAELE RLEHV
//
