(data stored in ACNUC29543 zone)

SWISSPROT: A5GQ28_SYNR3

ID   A5GQ28_SYNR3            Unreviewed;       361 AA.
AC   A5GQ28;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000256|RuleBase:RU004473};
DE            EC=4.2.1.46 {ECO:0000256|RuleBase:RU004473};
GN   Name=rfbB {ECO:0000313|EMBL:CAK26987.1};
GN   OrderedLocusNames=SynRCC307_0084 {ECO:0000313|EMBL:CAK26987.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK26987.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK26987.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-
CC         glucose + H2O; Xref=Rhea:RHEA:17221, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57477, ChEBI:CHEBI:57649; EC=4.2.1.46;
CC         Evidence={ECO:0000256|RuleBase:RU004473};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|RuleBase:RU004473};
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. dTDP-glucose dehydratase subfamily.
CC       {ECO:0000256|RuleBase:RU004473}.
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DR   EMBL; CT978603; CAK26987.1; -; Genomic_DNA.
DR   RefSeq; WP_011934502.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0084; -.
DR   EnsemblBacteria; CAK26987; CAK26987; SynRCC307_0084.
DR   KEGG; syr:SynRCC307_0084; -.
DR   eggNOG; ENOG4105C1B; Bacteria.
DR   eggNOG; COG1088; LUCA.
DR   HOGENOM; HOG000168006; -.
DR   KO; K01710; -.
DR   OMA; KLIPLMC; -.
DR   OrthoDB; 707977at2; -.
DR   BioCyc; SSP316278:G1GJL-84-MONOMER; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro.
DR   CDD; cd05246; dTDP_GD_SDR_e; 1.
DR   InterPro; IPR005888; dTDP_Gluc_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; TIGR01181; dTDP_gluc_dehyt; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GQ28.
DR   SWISS-2DPAGE; A5GQ28.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Lyase {ECO:0000256|RuleBase:RU004473, ECO:0000313|EMBL:CAK26987.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115}.
FT   DOMAIN       14    330       NAD(P)-bd_dom. {ECO:0000259|Pfam:
FT                                PF16363}.
SQ   SEQUENCE   361 AA;  39364 MW;  E106787C0BAE7F5D CRC64;
     MPDSLLPAGI NRVLVTGGAG FIGGAVVRRL LSDSDALVFN LDKCGYASDL ASIEALPEAK
     GRHQLLQLDL ADAEATAAAV QQADPDLVMH LAAESHVDRS IDGPGAFISS NVNGTFALLQ
     AARSHWEGLS EERRSRFRFH HISTDEVFGS LGATGRFSES TPYDPRSPYS ASKAASDHLV
     NAWHHTYGLP VVLTNCSNNY GPWQFPEKLI PVVILKAIAG EPIPLYGDGA NVRDWLYVED
     HVDALLLAAT RGQLGASYCV GGHGERSNRE VVETICQLLD ERRPEGAPHA RLITRVADRP
     GHDRRYAIDP ARISSELGWQ PRHDFNAGLA ATVDWYLQNQ QWCNSVRQRA GYSGERIGTR
     A
//

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