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Database: UniProt
Entry: A0A1G8SGL2_9BURK
LinkDB: A0A1G8SGL2_9BURK
Original site: A0A1G8SGL2_9BURK 
ID   A0A1G8SGL2_9BURK        Unreviewed;       345 AA.
AC   A0A1G8SGL2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-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=SAMN05444748_11210 {ECO:0000313|EMBL:SDJ28347.1};
OS   Variovorax sp. OV700.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1882826 {ECO:0000313|EMBL:SDJ28347.1, ECO:0000313|Proteomes:UP000199505};
RN   [1] {ECO:0000313|Proteomes:UP000199505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV700 {ECO:0000313|Proteomes:UP000199505};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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}.
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DR   EMBL; FNDR01000012; SDJ28347.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8SGL2; -.
DR   STRING; 1882826.SAMN05444748_11210; -.
DR   OrthoDB; 9779041at2; -.
DR   Proteomes; UP000199505; 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..331
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   345 AA;  38396 MW;  5DCE06445126F3FE CRC64;
     MKKHAVVTGI TGQDGAYLAE LLLAKGYVVY GAYRRTSSVN FWRIEELGIQ NNPDLHLVEH
     DLTDLGSSIA LIRDAAPDEV YNLAAQSFVG VSFNQPVATS QITGVGTLHL LEAIRLVNPK
     IRFYQASTSE MFGKVQAVPQ IEETPFYPRS PYGVAKLYAH WMTINYRESY GIFGCSGILF
     NHESPLRGRE FVTRKITDSV AKIKLGKLDV LELGNLNAKR DWGYAKEYVE GMWRMLQAQE
     PDTYVLATNR TETVRDFVTM AFKSAGMAIE FRGSGDSESA VDAATGKTVM RINPEFHRPA
     EVELLIGNPA KAKAKLGWEP ATTLEQLCQM MVEADLRRNV QGSSF
//
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