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Database: UniProt
Entry: A0A080M0Z4_9PROT
LinkDB: A0A080M0Z4_9PROT
Original site: A0A080M0Z4_9PROT 
ID   A0A080M0Z4_9PROT        Unreviewed;       374 AA.
AC   A0A080M0Z4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
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:KFB74927.1};
GN   ORFNames=AW06_004088 {ECO:0000313|EMBL:KFB74927.1};
OS   Candidatus Accumulibacter cognatus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=2954383 {ECO:0000313|EMBL:KFB74927.1, ECO:0000313|Proteomes:UP000021315};
RN   [1] {ECO:0000313|EMBL:KFB74927.1, ECO:0000313|Proteomes:UP000021315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-02 {ECO:0000313|Proteomes:UP000021315};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) 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:KFB74927.1}.
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DR   EMBL; JDST02000116; KFB74927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A080M0Z4; -.
DR   STRING; 1453999.AW06_004088; -.
DR   Proteomes; UP000021315; 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, ECO:0000313|EMBL:KFB74927.1};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00955};
KW   Reference proteome {ECO:0000313|Proteomes:UP000021315}.
FT   DOMAIN          9..348
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   374 AA;  42204 MW;  8D8C5FD8ECCF0222 CRC64;
     MITSQKVALI TGVTGQDGAY LAESLLDKGY QVHGIKRRSS LFNTDRIDHL YQDPHEPGRR
     FILHHGDLTD STSLIRIIQE VQPDEIYNLA AQSHVAVSFE EPEYTANADG IGALRMLEAI
     RILGLEKKSR FYQASTSELY GLVQESPQKE TTPFYPRSPY AVAKLYAYWI TVNYREAYGI
     YACNGILFNH ESPVRGETFV TRKITRAIAR IALGLQDCLY LGNLGALRDW GHARDYVEMQ
     WLMLQQDHPE DFVIATGVQY SVRQFVEFAA AELGMGVLFE GEGVNEIGIV TRVEGDKAKV
     RPGTVIVRVD PRYFRPTEVE TLLGDPRKAR EKLGWTPTTS LHELVKEMAL ADYNSARRDA
     LVKLAGFKAF DHNE
//
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