ID 6PGD_BUCBP Reviewed; 468 AA. AC Q89AX5; DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2003, sequence version 1. DT 02-SEP-2026, entry version 139. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44 {ECO:0000250|UniProtKB:P00350}; GN Name=gnd; OrderedLocusNames=bbp_101; OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Erwiniaceae; Buchnera. OX NCBI_TaxID=224915; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bp; RX PubMed=12522265; DOI=10.1073/pnas.0235981100; RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.; RT "Reductive genome evolution in Buchnera aphidicola."; RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003). 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|UniProtKB:P00350}. CC -!- CATALYTIC ACTIVITY: CC Reaction=6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO2 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 Evidence={ECO:0000250|UniProtKB:P00350}; CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 3/3. {ECO:0000250|UniProtKB:P00350}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00350}. 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; AE016826; AAO26836.1; -; Genomic_DNA. DR RefSeq; WP_011091237.1; NC_004545.1. DR AlphaFoldDB; Q89AX5; -. DR SMR; Q89AX5; -. DR STRING; 224915.bbp_101; -. DR KEGG; bab:bbp_101; -. DR eggNOG; COG0362; Bacteria. DR HOGENOM; CLU_024540_4_2_6; -. DR OrthoDB; 9804542at2; -. DR UniPathway; UPA00115; UER00410. DR Proteomes; UP000000601; Chromosome. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; ISS:UniProtKB. DR GO; GO:0006098; P:pentose-phosphate shunt; ISS:UniProtKB. DR FunFam; 1.10.1040.10:FF:000002; 6-phosphogluconate dehydrogenase, decarboxylating; 1. DR FunFam; 1.20.5.320:FF:000001; 6-phosphogluconate dehydrogenase, decarboxylating; 1. DR FunFam; 3.40.50.720:FF:000007; 6-phosphogluconate dehydrogenase, decarboxylating; 1. DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1. DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 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 NCBIfam; NF006765; PRK09287.1; 1. DR PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 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..468 FT /note="6-phosphogluconate dehydrogenase, decarboxylating" FT /id="PRO_0000090030" FT ACT_SITE 182 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P00350" FT ACT_SITE 189 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 14 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P96789" FT BINDING 33 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 34 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 35 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 38 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 74 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P96789" FT BINDING 75 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 102 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P96789" FT BINDING 128 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 129 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 130 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 182 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 186 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 189 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 190 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 259 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 286 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 445 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 451 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" SQ SEQUENCE 468 AA; 52646 MW; C28B8C09CCB64E11 CRC64; MAKQQIGVIG MAVMGRNLAL NMERNQYTVS IFNRSLDITE KIILNNPNKN LFPFFSIKDF VLSLIVPRCI VLMIKSGVAT DDTIKSLIPY LSKGDIIIDG GNTFYKDTIQ RGYELLKIGV NLIGAGFSGG EKGALYGPSI MPGGRQEAYN YVSPILKKIA SNSEGIPCVT YIGPDGSGHY VKMVHNGIEY GDMQLIAESY FILKTLLRLD NQSISKIFDI WNQGELNSYL IDITKDILIK KDDQNNYLID CILDEGSSKG TGTWTTKSAL DLNEPLTLIT ESVFFRYLSS LKSQRLLASK ILCGPKDFFI VLNRDDFIEK IRQALYLGKI ISYAQGFSQL NSASQKYNWN LKLGEISRIF QSGCIIRAKL LKNITQEYSS NNNFVNLLLT PYFREIANTY HSSLREIVSI SVKYGIPIPA LSSAISYFDS YRSAFLPSNL IQAQRDFFGA HTYKRIDKSG IFHTNWYS //