ID 6PGD_ECOLI Reviewed; 468 AA. AC P00350; P78080; Q47571; Q59366; Q59402; Q59411; Q59412; Q59413; Q59414; AC Q59416; Q79DT3; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 27-MAR-2024, entry version 191. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=gnd; OrderedLocusNames=b2029, JW2011; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6329905; DOI=10.1016/0378-1119(84)90070-2; RA Nasoff M.S., Baker H.V. II, Wolf R.E. Jr.; RT "DNA sequence of the Escherichia coli gene, gnd, for 6-phosphogluconate RT dehydrogenase."; RL Gene 27:253-264(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ECOR 10; RX PubMed=2050640; DOI=10.1128/jb.173.12.3894-3900.1991; RA Bisercic M., Feutrier J.Y., Reeves P.R.; RT "Nucleotide sequences of the gnd genes from nine natural isolates of RT Escherichia coli: evidence of intragenic recombination as a contributing RT factor in the evolution of the polymorphic gnd locus."; RL J. Bacteriol. 173:3894-3900(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ECOR 45, ECOR 65, ECOR 67, ECOR 68, ECOR 69, and ECOR 70; RX PubMed=1938920; DOI=10.1128/jb.173.22.7257-7268.1991; RA Dykhuizen D.E., Green L.; RT "Recombination in Escherichia coli and the definition of biological RT species."; RL J. Bacteriol. 173:7257-7268(1991). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097040; DOI=10.1093/dnares/3.6.379; RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., RA Horiuchi T.; RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 40.1-50.0 min region on the linkage map."; RL DNA Res. 3:379-392(1996). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125. RX PubMed=2464736; DOI=10.1093/oxfordjournals.molbev.a040522; RA Miller R.D., Dykhuizen D.E., Hartl D.L.; RT "Fitness effects of a deletion mutation increasing transcription of the 6- RT phosphogluconate dehydrogenase gene in Escherichia coli."; RL Mol. Biol. Evol. 5:691-703(1988). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125. RX PubMed=3275621; DOI=10.1128/jb.170.1.372-379.1988; RA Barcak G.J., Wolf R.E. Jr.; RT "Comparative nucleotide sequence analysis of growth-rate-regulated gnd RT alleles from natural isolates of Escherichia coli and from Salmonella RT typhimurium LT-2."; RL J. Bacteriol. 170:372-379(1988). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125. RC STRAIN=O7:K1 / VW187; RX PubMed=7677991; DOI=10.1128/jb.175.1.148-158.1993; RA Marolda C.L., Valvano M.A.; RT "Identification, expression, and DNA sequence of the GDP-mannose RT biosynthesis genes encoded by the O7 rfb gene cluster of strain VW187 RT (Escherichia coli O7:K1)."; RL J. Bacteriol. 175:148-158(1993). RN [10] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH NADP AND SUBSTRATE, RP SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, BIOPHYSICOCHEMICAL RP PROPERTIES, AND PATHWAY. RX PubMed=19686854; DOI=10.1016/j.jsb.2009.08.006; RA Chen Y.Y., Ko T.P., Chen W.H., Lo L.P., Lin C.H., Wang A.H.; RT "Conformational changes associated with cofactor/substrate binding of 6- RT phosphogluconate dehydrogenase from Escherichia coli and Klebsiella RT pneumoniae: Implications for enzyme mechanism."; RL J. Struct. Biol. 169:25-35(2010). 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:0000269|PubMed:19686854}. 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 Evidence={ECO:0000269|PubMed:19686854}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=49 uM for NADP {ECO:0000269|PubMed:19686854}; CC KM=93 uM for 6-phospho-D-gluconate {ECO:0000269|PubMed:19686854}; CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 3/3. {ECO:0000305|PubMed:19686854}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19686854}. CC -!- INTERACTION: CC P00350; P00350: gnd; NbExp=4; IntAct=EBI-907049, EBI-907049; 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; K02072; AAA23918.1; -; Genomic_DNA. DR EMBL; M63821; AAA24488.1; -; Genomic_DNA. DR EMBL; M64326; AAA24204.1; -; Genomic_DNA. DR EMBL; M64327; AAA24205.1; -; Genomic_DNA. DR EMBL; M64328; AAA24206.1; -; Genomic_DNA. DR EMBL; M64329; AAA24207.1; -; Genomic_DNA. DR EMBL; M64330; AAA24208.1; -; Genomic_DNA. DR EMBL; M64331; AAA24209.1; -; Genomic_DNA. DR EMBL; U00096; AAC75090.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15869.1; -; Genomic_DNA. DR EMBL; M23181; AAA23924.1; -; Genomic_DNA. DR EMBL; M18956; AAA23919.1; -; Genomic_DNA. DR EMBL; M18957; AAA23920.1; -; Genomic_DNA. DR EMBL; M18960; AAA23922.1; -; Genomic_DNA. DR EMBL; AF125322; AAC27540.1; -; Genomic_DNA. DR PIR; D64968; DEECGC. DR PIR; I62463; I62463. DR PIR; I62465; I62465. DR RefSeq; NP_416533.1; NC_000913.3. DR RefSeq; WP_000043484.1; NZ_LN832404.1. DR PDB; 2ZYA; X-ray; 1.60 A; A/B=1-468. DR PDB; 2ZYD; X-ray; 1.50 A; A/B=1-468. DR PDB; 3FWN; X-ray; 1.50 A; A/B=1-468. DR PDBsum; 2ZYA; -. DR PDBsum; 2ZYD; -. DR PDBsum; 3FWN; -. DR AlphaFoldDB; P00350; -. DR SMR; P00350; -. DR BioGRID; 4261354; 19. DR BioGRID; 850901; 1. DR DIP; DIP-9819N; -. DR IntAct; P00350; 6. DR STRING; 511145.b2029; -. DR jPOST; P00350; -. DR PaxDb; 511145-b2029; -. DR EnsemblBacteria; AAC75090; AAC75090; b2029. DR GeneID; 946554; -. DR KEGG; ecj:JW2011; -. DR KEGG; eco:b2029; -. DR PATRIC; fig|1411691.4.peg.223; -. DR EchoBASE; EB0406; -. DR eggNOG; COG0362; Bacteria. DR HOGENOM; CLU_024540_4_2_6; -. DR InParanoid; P00350; -. DR OMA; CVTHVGP; -. DR OrthoDB; 9804542at2; -. DR PhylomeDB; P00350; -. DR BioCyc; EcoCyc:6PGLUCONDEHYDROG-MONOMER; -. DR BioCyc; MetaCyc:6PGLUCONDEHYDROG-MONOMER; -. DR BRENDA; 1.1.1.44; 2026. DR SABIO-RK; P00350; -. DR UniPathway; UPA00115; UER00410. DR EvolutionaryTrace; P00350; -. DR PRO; PR:P00350; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0050661; F:NADP binding; IBA:GO_Central. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc. DR GO; GO:0046177; P:D-gluconate catabolic process; IMP:EcoCyc. DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:UniProtKB. 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 1: Evidence at protein level; KW 3D-structure; Gluconate utilization; NADP; Oxidoreductase; Pentose shunt; KW Reference proteome. FT CHAIN 1..468 FT /note="6-phosphogluconate dehydrogenase, decarboxylating" FT /id="PRO_0000090037" FT ACT_SITE 183 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:19686854" FT ACT_SITE 190 FT /note="Proton donor" FT /evidence="ECO:0000269|PubMed:19686854" FT BINDING 10..15 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT BINDING 33..35 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT BINDING 74..76 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" 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 BINDING 128..130 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" 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 BINDING 287 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT BINDING 445 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT BINDING 451 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT VARIANT 2 FT /note="S -> L (in strain: ECOR 70)" FT VARIANT 32 FT /note="F -> Y (in strain: ECOR 70)" FT VARIANT 39 FT /note="T -> Q (in strain: O7:K1 / VW187)" FT VARIANT 52 FT /note="V -> D (in strain: ECOR 10)" FT VARIANT 55 FT /note="Y -> F (in strain: ECOR 10)" FT VARIANT 102 FT /note="N -> K (in strain: ECOR 65)" FT VARIANT 117 FT /note="A -> S (in strain: ECOR 70)" FT VARIANT 123..125 FT /note="IGT -> YRY (in strain: O7:K1 / VW187)" FT VARIANT 170 FT /note="V -> F (in strain: ECOR 10)" FT VARIANT 175 FT /note="A -> S (in strain: ECOR 45)" FT VARIANT 209 FT /note="N -> S (in strain: ECOR 68)" FT VARIANT 211 FT /note="T -> S (in strain: ECOR 10 and ECOR 69)" FT VARIANT 216 FT /note="A -> T (in strain: ECOR 67)" FT VARIANT 294 FT /note="D -> E (in strain: ECOR 70)" FT VARIANT 308 FT /note="A -> G (in strain: ECOR 68)" FT VARIANT 313 FT /note="D -> N (in strain: ECOR 67)" FT VARIANT 315 FT /note="A -> G (in strain: ECOR 70)" FT VARIANT 325 FT /note="L -> Q (in strain: ECOR 69)" FT VARIANT 330 FT /note="I -> S (in strain: ECOR 10)" FT VARIANT 350 FT /note="D -> A (in strain: ECOR 10 and ECOR 69)" FT VARIANT 369 FT /note="Q -> R (in strain: ECOR 10)" FT VARIANT 422 FT /note="S -> A (in strain: ECOR 10, ECOR 65, ECOR 68, ECOR FT 69 and ECOR 70)" FT CONFLICT 306 FT /note="P -> R (in Ref. 1; AAA23918)" FT /evidence="ECO:0000305" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 13..23 FT /evidence="ECO:0007829|PDB:2ZYD" FT TURN 24..26 FT /evidence="ECO:0007829|PDB:2ZYD" FT STRAND 29..32 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 36..45 FT /evidence="ECO:0007829|PDB:2ZYD" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 57..62 FT /evidence="ECO:0007829|PDB:2ZYD" FT STRAND 69..72 FT /evidence="ECO:0007829|PDB:2ZYD" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 79..87 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:2ZYD" FT STRAND 96..99 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 105..117 FT /evidence="ECO:0007829|PDB:2ZYD" FT STRAND 121..129 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 130..136 FT /evidence="ECO:0007829|PDB:2ZYD" FT STRAND 139..144 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 146..159 FT /evidence="ECO:0007829|PDB:2ZYD" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 178..208 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 212..224 FT /evidence="ECO:0007829|PDB:2ZYD" FT TURN 225..227 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 230..240 FT /evidence="ECO:0007829|PDB:2ZYD" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 249..252 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 265..273 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 278..290 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 293..300 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 314..347 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 353..359 FT /evidence="ECO:0007829|PDB:2ZYD" FT STRAND 361..364 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 370..380 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 387..389 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 391..414 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 419..431 FT /evidence="ECO:0007829|PDB:2ZYD" FT HELIX 438..449 FT /evidence="ECO:0007829|PDB:2ZYD" FT STRAND 455..458 FT /evidence="ECO:0007829|PDB:2ZYD" FT STRAND 460..462 FT /evidence="ECO:0007829|PDB:3FWN" SQ SEQUENCE 468 AA; 51481 MW; 62A32C84DC596D86 CRC64; MSKQQIGVVG MAVMGRNLAL NIESRGYTVS IFNRSREKTE EVIAENPGKK LVPYYTVKEF VESLETPRRI LLMVKAGAGT DAAIDSLKPY LDKGDIIIDG GNTFFQDTIR RNRELSAEGF NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILTKIA AVAEDGEPCV TYIGADGAGH YVKMVHNGIE YGDMQLIAEA YSLLKGGLNL TNEELAQTFT EWNNGELSSY LIDITKDIFT KKDEDGNYLV DVILDEAANK GTGKWTSQSA LDLGEPLSLI TESVFARYIS SLKDQRVAAS KVLSGPQAQP AGDKAEFIEK VRRALYLGKI VSYAQGFSQL RAASEEYNWD LNYGEIAKIF RAGCIIRAQF LQKITDAYAE NPQIANLLLA PYFKQIADDY QQALRDVVAY AVQNGIPVPT FSAAVAYYDS YRAAVLPANL IQAQRDYFGA HTYKRIDKEG VFHTEWLD //