ID A0A1F6MEX9_9BACT Unreviewed; 334 AA.
AC A0A1F6MEX9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=A2754_00700 {ECO:0000313|EMBL:OGH70088.1};
OS Candidatus Magasanikbacteria bacterium RIFCSPHIGHO2_01_FULL_47_8.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798673 {ECO:0000313|EMBL:OGH70088.1, ECO:0000313|Proteomes:UP000177953};
RN [1] {ECO:0000313|EMBL:OGH70088.1, ECO:0000313|Proteomes:UP000177953}
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:OGH70088.1}.
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DR EMBL; MFPU01000016; OGH70088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6MEX9; -.
DR Proteomes; UP000177953; 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 7..316
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 334 AA; 38039 MW; CEAF1A4C7FB03EC5 CRC64;
MDKKVAFVTG ISGQDGSYLT EFLLNKGYEV HGIVRRSSSV FRERLEYLYP EHKDKNLFLY
YGDLANGSSL ARLLYKIQPH EIYNLAAQSH VKISFDIPEY TSDVVALGTI RLLEWVREND
SKTKFYQASS SEMFGKVLET PQKETTPFYP RSPYACAKVF AHYATVNYRE SYGAFACSGI
LFNHESPRRG ENFVTRKITK GIADILSKKT DKISLGNLDA RRDWGYAKDY VEAMWLMLQQ
DRPDDYVIAT GETHSVKEFA EEAFKVAGLD WEKYVVVDKK YFRPAEVDLL IGDASKAKQV
LGWTPKTGFK ELAKMMVKAD CAEAGVMIDN YVTT
//