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-MAY-2013, entry version 76.
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 (By similarity).
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 (By similarity).
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase
CC family.
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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; KQQIGVI; -.
DR ProtClustDB; PRK09287; -.
DR UniPathway; UPA00115; UER00410.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA: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; 6DGDH_C_like; 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 (By similarity).
FT NP_BIND 32 34 NADP (By similarity).
FT NP_BIND 73 75 NADP (By similarity).
FT REGION 127 129 Substrate binding (By similarity).
FT REGION 185 186 Substrate binding (By similarity).
FT ACT_SITE 182 182 Proton acceptor (By similarity).
FT ACT_SITE 189 189 Proton donor (By similarity).
FT BINDING 101 101 NADP (By similarity).
FT BINDING 101 101 Substrate (By similarity).
FT BINDING 190 190 Substrate (By similarity).
FT BINDING 259 259 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 286 286 Substrate (By similarity).
FT BINDING 444 444 Substrate; shared with dimeric partner
FT (By similarity).
FT BINDING 450 450 Substrate; shared with dimeric partner
FT (By similarity).
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
//
