ID   6PGD_STAEQ              Reviewed;         468 AA.
AC   Q5HP42;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-NOV-2008, entry version 29.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE            EC=1.1.1.44;
GN   Name=gnd; OrderedLocusNames=SERP1071;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA   Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA   Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA   Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA   Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA   Hance I.R., Nelson K.E., Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete
RT   genome analysis of an early methicillin-resistant Staphylococcus
RT   aureus strain and a biofilm-producing methicillin-resistant
RT   Staphylococcus epidermidis strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase
CC       family.
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DR   EMBL; CP000029; AAW54437.1; -; Genomic_DNA.
DR   RefSeq; YP_188648.1; -.
DR   GeneID; 3242766; -.
DR   GenomeReviews; CP000029_GR; SERP1071.
DR   KEGG; ser:SERP1071; -.
DR   TIGR; SERP1071; -.
DR   HOGENOM; Q5HP42; -.
DR   BioCyc; SEPI176279:SERP1071-MON; -.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxyla...; IEA:InterPro.
DR   GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro.
DR   InterPro; IPR006183; 6-phosphogluconate_DHase.
DR   InterPro; IPR006114; 6PGDH_C.
DR   InterPro; IPR006113; 6PGDH_decarbox.
DR   InterPro; IPR006115; 6PGDH_NAD-bd.
DR   InterPro; IPR006184; 6PGdom_BS.
DR   InterPro; IPR013328; DHase_multihelical.
DR   InterPro; IPR012284; Fibritin/6PGD_C-extension.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:1.20.5.320; Fibritin/6PGD_C-extension; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1.
DR   Pfam; PF00393; 6PGD; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PRINTS; PR00076; 6PGDHDRGNASE.
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_0000090059.
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
//