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 27-MAR-2024, entry version 135. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=gnd; OrderedLocusNames=TC_0333; OS Chlamydia muridarum (strain MoPn / Nigg). OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=243161; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MoPn / Nigg; RX PubMed=10684935; DOI=10.1093/nar/28.6.1397; RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., RA Salzberg S.L., Eisen J.A., Fraser C.M.; RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae RT AR39."; RL Nucleic Acids Res. 28:1397-1406(2000). CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate CC to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP CC to NADPH. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate CC + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44; CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 3/3. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE002160; AAF39196.1; -; Genomic_DNA. DR PIR; A81714; A81714. DR AlphaFoldDB; Q9PKX7; -. DR SMR; Q9PKX7; -. DR KEGG; cmu:TC_0333; -. DR eggNOG; COG0362; Bacteria. DR HOGENOM; CLU_024540_4_2_0; -. DR OrthoDB; 9804542at2; -. DR UniPathway; UPA00115; UER00410. DR Proteomes; UP000000800; Chromosome. 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:0016054; P:organic acid catabolic process; IEA:UniProt. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR013328; 6PGD_dom2. DR InterPro; IPR006114; 6PGDH_C. DR InterPro; IPR006113; 6PGDH_Gnd/GntZ. DR InterPro; IPR006115; 6PGDH_NADP-bd. DR InterPro; IPR006184; 6PGdom_BS. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR006183; Pgluconate_DH. DR NCBIfam; TIGR00873; gnd; 1. DR PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1. DR PANTHER; PTHR11811:SF25; 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000109; 6PGD; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR SMART; SM01350; 6PGD; 1. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00461; 6PGD; 1. PE 3: Inferred from homology; KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1..479 FT /note="6-phosphogluconate dehydrogenase, decarboxylating" FT /id="PRO_0000090031" FT ACT_SITE 183 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 190 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 10..15 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 33..35 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 75..77 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 103 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 103 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 129..131 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 186..187 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 191 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 260 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 287 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 447 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" FT BINDING 453 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" 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 //