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 27-MAR-2024, entry version 138. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=gnd; OrderedLocusNames=CT_063; OS Chlamydia trachomatis (strain D/UW-3/Cx). OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=272561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D/UW-3/Cx; RX 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., Davis R.W.; RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia RT trachomatis."; RL Science 282:754-759(1998). 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; AE001273; AAC67654.1; -; Genomic_DNA. DR PIR; A71561; A71561. DR RefSeq; NP_219566.1; NC_000117.1. DR RefSeq; WP_010725014.1; NC_000117.1. DR AlphaFoldDB; O84066; -. DR SMR; O84066; -. DR STRING; 272561.CT_063; -. DR EnsemblBacteria; AAC67654; AAC67654; CT_063. DR GeneID; 884061; -. DR KEGG; ctr:CT_063; -. DR PATRIC; fig|272561.5.peg.72; -. DR HOGENOM; CLU_024540_4_2_0; -. DR InParanoid; O84066; -. DR OrthoDB; 9804542at2; -. DR UniPathway; UPA00115; UER00410. DR Proteomes; UP000000431; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0050661; F:NADP binding; IBA:GO_Central. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IBA:GO_Central. DR GO; GO:0046177; P:D-gluconate catabolic process; IBA:GO_Central. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central. 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; KW Reference proteome. FT CHAIN 1..480 FT /note="6-phosphogluconate dehydrogenase, decarboxylating" FT /id="PRO_0000090033" FT ACT_SITE 184 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 191 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 11..16 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 34..36 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 76..78 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 104 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 104 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 130..132 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 187..188 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 192 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 261 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 288 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 448 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" FT BINDING 454 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" 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 //