ID 6PGD_BUCAP Reviewed; 473 AA. AC Q9ZHD9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2002, sequence version 2. DT 27-MAR-2024, entry version 145. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=gnd; OrderedLocusNames=BUsg_100; OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=198804; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9767718; DOI=10.1007/s002849900392; RA Clark M.A., Baumann L., Baumann P.; RT "Buchnera aphidicola (Aphid endosymbiont) contains genes encoding enzymes RT of histidine biosynthesis."; RL Curr. Microbiol. 37:356-358(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sg; RX PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). 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; AF067228; AAC97362.1; -; Genomic_DNA. DR EMBL; AE013218; AAM67670.1; -; Genomic_DNA. DR RefSeq; WP_011053636.1; NC_004061.1. DR AlphaFoldDB; Q9ZHD9; -. DR SMR; Q9ZHD9; -. DR STRING; 198804.BUsg_100; -. DR GeneID; 75259024; -. DR KEGG; bas:BUsg_100; -. DR eggNOG; COG0362; Bacteria. DR HOGENOM; CLU_024540_4_2_6; -. DR UniPathway; UPA00115; UER00410. DR Proteomes; UP000000416; Chromosome. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; ISS:UniProtKB. 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; ISS:UniProtKB. 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:SF63; 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING 2; 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..473 FT /note="6-phosphogluconate dehydrogenase, decarboxylating" FT /id="PRO_0000090029" FT ACT_SITE 182 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 189 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 74..76 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 102 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 102 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 128..130 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 185..186 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 190 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 446 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" FT BINDING 452 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" FT CONFLICT 158 FT /note="K -> N (in Ref. 1; AAC97362)" FT /evidence="ECO:0000305" FT CONFLICT 324..326 FT /note="RRA -> TKS (in Ref. 1; AAC97362)" FT /evidence="ECO:0000305" FT CONFLICT 348 FT /note="K -> I (in Ref. 1; AAC97362)" FT /evidence="ECO:0000305" SQ SEQUENCE 473 AA; 53805 MW; A11842A037E1E984 CRC64; MLKQQVGVIG MAVMGRNLAL NIESKKYTVS IFNRTQSVTE EVINNNKEKK IFPYFSIKDF VNSLRKPRCI LLMVKSGQPT DETIQFILPY LNKGDILIDG GNTFYKDSIR RSNDLMKCGI NFIGMGVSGG ELGALNGPSI MPGGSREAYD LVSSMLKKIS AKFKNEPCVS YIGPNGAGHY VKMIHNGIEY GDMQLISESY FILKNVLNMK NEELSNTFSQ WNKGELNSYL IEITKNIFLK KEKDGIHYLI DSILDHAEDK GTGKWISQDA LELHEPLSLI TESVFARYLS SLKDQRLIAS KILKGPILKC ISSQNKELFV EEVRRALYLG KIISYAQGFS QLKKASEKYS WNLQYGKIAK IFRAGCIIRA DFLERITDAF KSNNVTNLLL TPYFSEISNK YEKSLRYITS YAIKYGIPVP TFASAISYYD NYRTMSSSAN LIQAQRDYFG AHTYRRTDKK GYFHTNWLTK KEL //