GenomeNet

Database: UniProt
Entry: Q8CP47
LinkDB: Q8CP47
Original site: Q8CP47 
ID   6PGD_STAES              Reviewed;         468 AA.
AC   Q8CP47;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   01-OCT-2014, entry version 81.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE            EC=1.1.1.44;
GN   Name=gnd; OrderedLocusNames=SE_1192;
OS   Staphylococcus epidermidis (strain ATCC 12228).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J.,
RA   Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA   Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-
CC       phosphogluconate to ribulose 5-phosphate and CO(2), with
CC       concomitant reduction of NADP to NADPH. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose
CC       5-phosphate + CO(2) + NADPH.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC       step 3/3.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase
CC       family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE015929; AAO04791.1; -; Genomic_DNA.
DR   RefSeq; NP_764747.1; NC_004461.1.
DR   ProteinModelPortal; Q8CP47; -.
DR   SMR; Q8CP47; 6-465.
DR   STRING; 176280.SE1192; -.
DR   PRIDE; Q8CP47; -.
DR   EnsemblBacteria; AAO04791; AAO04791; SE_1192.
DR   GeneID; 1057829; -.
DR   KEGG; sep:SE1192; -.
DR   PATRIC; 19608178; VBIStaEpi113981_1162.
DR   eggNOG; COG0362; -.
DR   KO; K00033; -.
DR   OMA; RVASENY; -.
DR   OrthoDB; EOG6MSS4W; -.
DR   BioCyc; SEPI176280:GCDG-1198-MONOMER; -.
DR   UniPathway; UPA00115; UER00410.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   Gene3D; 1.20.5.320; -; 1.
DR   Gene3D; 3.40.50.720; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR006114; 6PGDH_C.
DR   InterPro; IPR006113; 6PGDH_decarbox.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR006184; 6PGdom_BS.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR012284; Fibritin/6PGD_C-extension.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF00393; 6PGD; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000109; 6PGD; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   TIGRFAMs; TIGR00873; gnd; 1.
DR   PROSITE; PS00461; 6PGD; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Gluconate utilization; NADP; Oxidoreductase;
KW   Pentose shunt.
FT   CHAIN         1    468       6-phosphogluconate dehydrogenase,
FT                                decarboxylating.
FT                                /FTId=PRO_0000090058.
FT   NP_BIND       9     14       NADP. {ECO:0000250}.
FT   NP_BIND      32     34       NADP. {ECO:0000250}.
FT   NP_BIND      73     75       NADP. {ECO:0000250}.
FT   REGION      127    129       Substrate binding. {ECO:0000250}.
FT   REGION      185    186       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    182    182       Proton acceptor. {ECO:0000250}.
FT   ACT_SITE    189    189       Proton donor. {ECO:0000250}.
FT   BINDING     101    101       NADP. {ECO:0000250}.
FT   BINDING     101    101       Substrate. {ECO:0000250}.
FT   BINDING     190    190       Substrate. {ECO:0000250}.
FT   BINDING     259    259       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     286    286       Substrate. {ECO:0000250}.
FT   BINDING     444    444       Substrate; shared with dimeric partner.
FT                                {ECO:0000250}.
FT   BINDING     450    450       Substrate; shared with dimeric partner.
FT                                {ECO:0000250}.
SQ   SEQUENCE   468 AA;  52234 MW;  A4738F224237494E CRC64;
     MTQQIGVVGL AVMGKNLAWN IESRGYSVSV YNRSRQKTDE MVKESPGREI YPTYSLEEFV
     ESLEKPRKIL LMVKAGPATD ATIDGLLPLL DDDDILIDGG NTNYQDTIRR NKALAESSIN
     FIGMGVSGGE IGALTGPSLM PGGQKDAYNK VSDILDAIAA KAQDGASCVT YIGPNGAGHY
     VKMVHNGIEY ADMQLIAESY AMMKDLLGMS HKEISQTFKE WNAGELESYL IEITGDIFNK
     LDDDNEALVE KILDTAGQKG TGKWTSINAL ELGVPLTIIT ESVFARFISS IKEERVTASK
     SLKGPKAHFE GDKKTFLEKI RKALYMSKIC SYAQGFAQMR KASEDNEWNL KLGELAMIWR
     EGCIIRAQFL QKIKDAYDNN ENLQNLLLDP YFKNIVMEYQ DALREVVATS VYNGVPTPGF
     SASINYYDSY RSEDLPANLI QAQRDYFGAH TYERKDREGI FHTQWVEE
//
DBGET integrated database retrieval system