ID   6PGD_CHLMU              Reviewed;         479 AA.
AC   Q9PKX7;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-NOV-2008, entry version 52.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE            EC=1.1.1.44;
GN   Name=gnd; OrderedLocusNames=TC_0333;
OS   Chlamydia muridarum.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=83560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   MEDLINE=20150255; PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F.,
RA   White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J.,
RA   Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C.,
RA   Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F.,
RA   McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia
RT   pneumoniae AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39196.1; -; Genomic_DNA.
DR   PIR; A81714; A81714.
DR   RefSeq; NP_296712.1; -.
DR   HSSP; P00349; 2PGD.
DR   GeneID; 1246377; -.
DR   GenomeReviews; AE002160_GR; TC_0333.
DR   KEGG; cmu:TC0333; -.
DR   TIGR; TC_0333; -.
DR   HOGENOM; Q9PKX7; -.
DR   BioCyc; CMUR243161:TC_0333-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    479       6-phosphogluconate dehydrogenase,
FT                                decarboxylating.
FT                                /FTId=PRO_0000090031.
SQ   SEQUENCE   479 AA;  52689 MW;  3501DD6DAA0B8F8B CRC64;
     MAPADIGLIG LAVMGKNLVL NMIDHGFAVS VYNRSPEKTE EFLKEHGENI SLQGFTAIEE
     FVQSLKRPRK IMIMIKAGAP VDEMISSLLP FLEEGDILID GGNSYYLDSE RRYIDLKKKG
     ILFVGMGVSG GEEGARKGPS IMPGGNIEAW PVIAPIFQSI AAQVDGQPCC SWIGTGGAGH
     FVKAVHNGIE YGDIQLICET YEILKSRLDL SLEQIGNIFF EWNQTDLNSY LMGASAAVLT
     AKDENGVAVA STILDVAGQK GTGRWVAEDA IKAGVPMSLI IESVLARYLS AWKEVRRQAA
     REFPVASLLY QPSQEASVLI EDAREALYAA KIISYAQGFM LLKQISEERN WDLNLGELAL
     IWRGGCIIQS AFLDKIHQGF ESCPDAHSLM LQDYFKNVLL NSETGFRRAI LHAVGAGVAI
     PCLASALAFY DGYRTENSPL FLVQGLRDYF GAHGYERQDR PRGEFYHTDW LGSKNASRM
//