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Database: UniProt
Entry: A0A257M3P0_9BACT
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ID   A0A257M3P0_9BACT        Unreviewed;       344 AA.
AC   A0A257M3P0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-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   ECO:0000313|EMBL:OYV06563.1};
GN   ORFNames=CFE26_05645 {ECO:0000313|EMBL:OYV06563.1};
OS   Verrucomicrobiales bacterium VVV1.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales.
OX   NCBI_TaxID=2015575 {ECO:0000313|EMBL:OYV06563.1, ECO:0000313|Proteomes:UP000216473};
RN   [1] {ECO:0000313|EMBL:OYV06563.1, ECO:0000313|Proteomes:UP000216473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VVV1 {ECO:0000313|EMBL:OYV06563.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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}.
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:OYV06563.1}.
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DR   EMBL; NKJB01000131; OYV06563.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257M3P0; -.
DR   Proteomes; UP000216473; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216473}.
FT   DOMAIN          5..318
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
FT   BINDING         127
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00955"
SQ   SEQUENCE   344 AA;  39397 MW;  F9FF258DCAD39EDB CRC64;
     MKRALITGIT GQDGSYLAEL LLEKGYEVHG IIRRSSTFNT DRIDHIYKDP HLNDARMLLH
     YGDLADGTNL AKLLNEIRPD EVYNLAAQSH VRVSYDAPEY TGDVTGLGAQ RLLEAIRQTG
     LIEKVRYYQA SSSEMFGKVQ EIPQTETTPF WPRSPYACAK VYAHWLTVNY REGYGLYGCN
     GILFNHESPR RGETFVTRKI TRAAGRIKMG LQDKLFLGNL DAKRDWGFAK EYVEMMWLML
     QQDQPDDYVV ATNETHSVKE FVQATFARLD LDWEKYVDYD DRYERPAEVD LLIGDPAKAK
     RQLGWEPKVK FKELVDIMTD ADLELARQEH AFASATGKPL SPVR
//
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