ID 6PGD_CHLTR Reviewed; 480 AA. AC O84066; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 16-JUN-2009, entry version 57. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=gnd; OrderedLocusNames=CT_063; OS Chlamydia trachomatis. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia. OX NCBI_TaxID=813; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D/UW-3/Cx; RX MEDLINE=99000809; PubMed=9784136; DOI=10.1126/science.282.5389.754; RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., RA Davis R.W.; RT "Genome sequence of an obligate intracellular pathogen of humans: RT Chlamydia trachomatis."; RL Science 282:754-759(1998). 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. 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; AE001273; AAC67654.1; -; Genomic_DNA. DR PIR; A71561; A71561. DR RefSeq; NP_219566.1; -. DR HSSP; P00349; 2PGD. DR GeneID; 884061; -. DR GenomeReviews; AE001273_GR; CT_063. DR KEGG; ctr:CT063; -. DR HOGENOM; O84066; -. DR OMA; O84066; PRKVMLM. DR BioCyc; CTRA315277:CT063-MON; -. DR BRENDA; 1.1.1.44; 108. DR GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxyla...; IEA:EC. 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:UniProtKB-KW. DR InterPro; IPR006183; 6-phosphogluconate_DH. DR InterPro; IPR006114; 6PGDH_C. DR InterPro; IPR006113; 6PGDH_decarbox. DR InterPro; IPR006115; 6PGDH_NAD-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 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 1 480 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090033. SQ SEQUENCE 480 AA; 52667 MW; E2D9BFE893DCECB2 CRC64; MAPNTDIGLI GLAVMGKNLV LNMVDHGFSV SVYNRSPAKT EEFLKDHGES GALQGFTTIQ EFVQSLKRPR KIMIMIKAGA PVDEMIASLL PFLEEGDILI DGGNSYYLDS EQRYVDLKKE GILFVGMGVS GGEEGARKGP SIMPGGNIDA WPAIAPIFQS IAAQVDGRPC CSWIGTGGAG HFVKAVHNGI EYGDIQLICE TYEILKTRLN LSLEQIGNIF FEWNQTDLNS YLIGAAAAVL IAKDENGNAI ASTILDVAGQ KGTGRWVAED AIKAGVPMSL IIESVLARYL STWKEVRTKA AQEFPGIPLL CQPPQEASAF IEDVREALYA AKIISYAQGF MLLKQVSQDK GWDLNLGELA LIWRGGCIIQ SAFLDKIHQG FENSPEAHSL ILQDYFKKVL FDSETGFRRA VLHAIGSGVA IPCLSSALSF YDGYRTVDSS LFLVQGLRDY FGAHGYERRD CPRGEFYHTD WLETKKTFRV //