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Database: UniProt
Entry: A0A1S9PEW8_9SPHI
LinkDB: A0A1S9PEW8_9SPHI
Original site: A0A1S9PEW8_9SPHI 
ID   A0A1S9PEW8_9SPHI        Unreviewed;       370 AA.
AC   A0A1S9PEW8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=BC343_04620 {ECO:0000313|EMBL:OOQ59470.1};
OS   Mucilaginibacter pedocola.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1792845 {ECO:0000313|EMBL:OOQ59470.1, ECO:0000313|Proteomes:UP000189739};
RN   [1] {ECO:0000313|EMBL:OOQ59470.1, ECO:0000313|Proteomes:UP000189739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBZ30 {ECO:0000313|EMBL:OOQ59470.1,
RC   ECO:0000313|Proteomes:UP000189739};
RA   Huang J., Tang J.;
RT   "Genomic analysis of zinc-resistant bacterium Mucilaginibacter pedocola
RT   TBZ30.";
RL   Submitted (JUL-2016) 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:OOQ59470.1}.
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DR   EMBL; MBTF01000012; OOQ59470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9PEW8; -.
DR   STRING; 1792845.BC343_04620; -.
DR   OrthoDB; 9779041at2; -.
DR   Proteomes; UP000189739; 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:UP000189739}.
FT   DOMAIN          5..344
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   370 AA;  41807 MW;  7D391B61557514FD CRC64;
     MKKALITGIT GQDGAYLADF LLKKGYEIHG IKRRSSSFNT DRIDNLYKDP HESDVRFKLH
     YGDLTDSTNL IRIIQQVQPD EIYNLGAMSH VKVSFDTPEY TANADGIGTL RLLEALRILG
     LEKKTKIYQA STSELYGLVQ AVPQSESTPF YPRSPYAVAK LYAYWITVNY REAYGMFACN
     GILFNHESPL RGETFVTRKI TRAVAKIALG LQEKLFLGNL NAQRDWGHAK DYVEAMYLIL
     QQEVAEDYVI ATGVTTAVRE FVRLAFNEVG ITVDFKGEGA DEKGYVVACS NPAYQVAIGT
     EVVSVDPRYF RPTEVELLVG DPTKSFEKLG WKPKYDLRGL IEDMMQSDIN LFKKDALLKE
     HGYVVKNQFE
//
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