ID A0A1G0YBT8_9BACT Unreviewed; 321 AA.
AC A0A1G0YBT8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=A2X46_06765 {ECO:0000313|EMBL:OGV43329.1};
OS Lentisphaerae bacterium GWF2_57_35.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798576 {ECO:0000313|EMBL:OGV43329.1, ECO:0000313|Proteomes:UP000178598};
RN [1] {ECO:0000313|EMBL:OGV43329.1, ECO:0000313|Proteomes:UP000178598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV43329.1}.
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DR EMBL; MHBK01000048; OGV43329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0YBT8; -.
DR STRING; 1798576.A2X46_06765; -.
DR Proteomes; UP000178598; 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 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};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00955}.
FT DOMAIN 4..308
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 321 AA; 36628 MW; E75743DCFC86B714 CRC64;
MKALITGITG QDGSYLADFL LEKGYEVYGM VRRSSTETFE RIAHIKDRLN LRQADLLDQL
SLIKLLEEVQ PDEIYNLAAM SFVPTSWNQP MLTGEYTAIG VTRLLEAVRL ICPKARFYQA
SSSEMFGKVR EVPQVETTPF HPRSPYGVAK AYGHYITVNY RESYGLFALS GILFNHESPR
RGKEFVTRKI SDAVAQIKLG FAKELRMGNV DAQRDWGFAG DYIRAMWMML QMEEPDDFVI
STGVSHSVKE FLEAAFSHVG LHWQDYVVED PSLFRPAEVD HLLGSSAKAE RVLGWKPHVD
FKGLVRMMVD ADMERWKQVK K
//
