(data stored in SCRATCH zone)

SWISSPROT: A5GQG1_SYNR3

ID   A5GQG1_SYNR3            Unreviewed;       368 AA.
AC   A5GQG1;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=GDP-mannose 4,6-dehydratase {ECO:0000256|HAMAP-Rule:MF_00955};
DE            EC=4.2.1.47 {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:CAK27120.1};
GN   OrderedLocusNames=SynRCC307_0217 {ECO:0000313|EMBL:CAK27120.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27120.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK27120.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RA   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-
CC       dehydro-6-deoxy-D-mannose. {ECO:0000256|HAMAP-Rule:MF_00955}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose +
CC         H2O; 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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00955};
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. GDP-mannose 4,6-dehydratase subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00955}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00955}.
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DR   EMBL; CT978603; CAK27120.1; -; Genomic_DNA.
DR   RefSeq; WP_011934635.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0217; -.
DR   EnsemblBacteria; CAK27120; CAK27120; SynRCC307_0217.
DR   KEGG; syr:SynRCC307_0217; -.
DR   eggNOG; ENOG4105C0K; Bacteria.
DR   eggNOG; COG1089; LUCA.
DR   HOGENOM; HOG000168003; -.
DR   KO; K01711; -.
DR   OMA; TDCLYLG; -.
DR   OrthoDB; 955232at2; -.
DR   BioCyc; SSP316278:G1GJL-213-MONOMER; -.
DR   Proteomes; UP000001115; 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   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   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01472; gmd; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GQG1.
DR   SWISS-2DPAGE; A5GQG1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00955, ECO:0000313|EMBL:CAK27120.1};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00955};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115}.
FT   DOMAIN       11    342       NAD(P)-bd_dom. {ECO:0000259|Pfam:
FT                                PF16363}.
SQ   SEQUENCE   368 AA;  41683 MW;  D351CE591E4D2D66 CRC64;
     MSSDQSRKTA LITGITGQDG SYLAELLLEK GYEVHGIKRR ASSFNTDRID HLYQDPHEND
     PRLVLHYGDL TDSTNLIRIV QQVQPDEIYN LGAQSHVAVS FESPEYTANS DALGTLRILE
     AVRILGLTNK TRIYQASTSE LYGLVQEIPQ KESTPFYPRS PYGVAKLYAY WITVNYRESY
     GMYACNGVLF NHESPRRGET FVTRKITRGL ARIDAGLDDC LYMGNLDSLR DWGHARDYVE
     MQWRMLQQDK PEDFVIATGR QESVRCFIEL TALELGWGAM QWEGKGIDEV GCRADTGDVV
     VKIDPRYFRP AEVETLLGDP TKAKEKLGWT PTTTLEELVA EMVATDKEEA QKEAYLKRKG
     FNVVGARE
//

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