ID 6PGD_HAEDU Reviewed; 484 AA. AC Q7VMX4; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 124. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=gnd; OrderedLocusNames=HD_0833; OS Haemophilus ducreyi (strain 35000HP / ATCC 700724). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=233412; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=35000HP / ATCC 700724; RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., RA Nguyen D., Wang J., Forst C., Hood L.; RT "The complete genome sequence of Haemophilus ducreyi."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. 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; AE017143; AAP95728.1; -; Genomic_DNA. DR RefSeq; WP_010944778.1; NC_002940.2. DR AlphaFoldDB; Q7VMX4; -. DR SMR; Q7VMX4; -. DR STRING; 233412.HD_0833; -. DR KEGG; hdu:HD_0833; -. DR eggNOG; COG0362; Bacteria. DR HOGENOM; CLU_024540_4_2_6; -. DR OrthoDB; 9804542at2; -. DR UniPathway; UPA00115; UER00410. DR Proteomes; UP000001022; 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; KW Reference proteome. FT CHAIN 1..484 FT /note="6-phosphogluconate dehydrogenase, decarboxylating" FT /id="PRO_0000090040" FT ACT_SITE 185 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 192 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 188..189 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 193 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 262 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 289 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 484 AA; 53272 MW; BA23A9A770615B23 CRC64; MSIKGDIGVI GLAVMGQNLI LNMNDNGFKV VAYNRTASKV DEFLAGEAKD TNIIGAYSLE DLAAKLEKPR KIMLMVRAGE VVDQFIDALL PHLEAGDIII DGGNSNYPDT NRRTITLAEK GIRFIGTGVS GGEEGARHGP SIMPGGNEEA WPFVKPILQA ISAKTDKDEP CCDWVGKEGA GHFVKMVHNG IEYGDMQLIC EAYQFLKDGL GLNYEEMHAI FADWKNTELD SYLIDITADI LAYKDADGEP LVEKILDTAG QKGTGKWTGI NALDFGIPLT LITEAVFARC VSAFKDQRVA VSQLFNKTIT PISDDKKEWI EAVRKALLAS KIISYAQGFM LIREASENFE WNINYGATAL LWREGCIIRS AFLGNIRDAY EANPGLVFLG SDPYFQNILQ SAMADWRKVV AKSIEIGIPM PCMAAAITFL DGYSSEHLPA NLLQAQRDYF GAHTYERTDK PRCSFFHTNW TGRGGNTAST TYDV //