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Database: UniProt
Entry: B7JBH0_ACIF2
LinkDB: B7JBH0_ACIF2
Original site: B7JBH0_ACIF2 
ID   B7JBH0_ACIF2            Unreviewed;       343 AA.
AC   B7JBH0;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
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-2 {ECO:0000313|EMBL:ACK78344.1};
GN   Synonyms=gmd {ECO:0000256|HAMAP-Rule:MF_00955};
GN   OrderedLocusNames=AFE_3292 {ECO:0000313|EMBL:ACK78344.1};
OS   Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS   / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC   Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=243159 {ECO:0000313|EMBL:ACK78344.1, ECO:0000313|Proteomes:UP000001362};
RN   [1] {ECO:0000313|EMBL:ACK78344.1, ECO:0000313|Proteomes:UP000001362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455
RC   {ECO:0000313|Proteomes:UP000001362};
RX   PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA   Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R.II.,
RA   Eisen J.A., Holmes D.S.;
RT   "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT   industrial applications.";
RL   BMC Genomics 9:597-597(2008).
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}.
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DR   EMBL; CP001219; ACK78344.1; -; Genomic_DNA.
DR   RefSeq; WP_012537699.1; NC_011761.1.
DR   AlphaFoldDB; B7JBH0; -.
DR   STRING; 243159.AFE_3292; -.
DR   PaxDb; 243159-AFE_3292; -.
DR   GeneID; 66434223; -.
DR   KEGG; afr:AFE_3292; -.
DR   eggNOG; COG1089; Bacteria.
DR   HOGENOM; CLU_007383_14_0_6; -.
DR   Proteomes; UP000001362; Chromosome.
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, ECO:0000313|EMBL:ACK78344.1};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00955};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001362}.
FT   DOMAIN          6..329
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   343 AA;  38467 MW;  D5CE6F8D2F6C0D01 CRC64;
     MTKHALITGI TGQDGAYLAQ WLLEKDYTVY GLIARRGTDT TGRLHELGIA DQVRLLDGDL
     IDLSSMIRAM EKSQATEVYN LGAQSFVATS WDQPILTAEV TGTSVVKMLE AIRIVNPQAR
     FYQASTSEMF GQIQEPLQSE RTPFHPRSPY GVAKLYGHWI TVNYRESFGL HASSGILFNH
     ESPLRGTEFV TRKITLALAR IRQGVQDVLE LGNLDSKRDW GYAGDYVRAM WLMLQQEQPD
     DYVIATGETW TVRTFVEKAA AHAGFDLEWR GEAEKTQGVD RRSGKVIVRV NPAFYRPAEV
     DILIGDPGKA QQKLGWKREV GFDALVRMMA EADLRRVAGE VVE
//
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