POXB_ECOLI
ID POXB_ECOLI Reviewed; 572 AA.
AC P07003; Q47513; Q47514; Q47515; Q47516; Q47517; Q47518; Q47519; Q47520;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Pyruvate dehydrogenase [ubiquinone] {ECO:0000255|HAMAP-Rule:MF_00850};
DE EC=1.2.5.1 {ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:18988747, ECO:0000269|PubMed:2663858};
DE AltName: Full=Pyruvate oxidase {ECO:0000255|HAMAP-Rule:MF_00850};
DE Short=POX {ECO:0000255|HAMAP-Rule:MF_00850};
DE AltName: Full=Pyruvate:ubiquinone-8 oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00850};
GN Name=poxB {ECO:0000255|HAMAP-Rule:MF_00850};
GN OrderedLocusNames=b0871, JW0855;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3016647; DOI=10.1093/nar/14.13.5449;
RA Grabau C., Cronan J.E. Jr.;
RT "Nucleotide sequence and deduced amino acid sequence of Escherichia coli
RT pyruvate oxidase, a lipid-activated flavoprotein.";
RL Nucleic Acids Res. 14:5449-5460(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP MUTAGENESIS OF ALA-533; ALA-553; ASP-560; 564-GLU--ARG-572; GLU-564;
RP 570-TRP--ARG-572 AND ARG-572, AND LIPID-BINDING.
RC STRAIN=K12;
RX PubMed=2663858; DOI=10.1016/s0021-9258(18)63887-6;
RA Grabau C., Chang Y.Y., Cronan J.E. Jr.;
RT "Lipid binding by Escherichia coli pyruvate oxidase is disrupted by small
RT alterations of the carboxyl-terminal region.";
RL J. Biol. Chem. 264:12510-12519(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 550-572, PROTEIN SEQUENCE OF 1-20 AND
RP 550-570, AND ACTIVATION BY PROTEOLYTIC CLEAVAGE IN VITRO.
RC STRAIN=K12;
RX PubMed=3902830; DOI=10.1016/s0021-9258(17)38715-x;
RA Recny M.A., Grabau C., Cronan J.E. Jr., Hager L.P.;
RT "Characterization of the alpha-peptide released upon protease activation of
RT pyruvate oxidase.";
RL J. Biol. Chem. 260:14287-14291(1985).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22, AND INDUCTION.
RX PubMed=8022274; DOI=10.1111/j.1365-2958.1994.tb00380.x;
RA Chang Y.Y., Wang A.Y., Cronan J.E. Jr.;
RT "Expression of Escherichia coli pyruvate oxidase (PoxB) depends on the
RT sigma factor encoded by the rpoS(katF) gene.";
RL Mol. Microbiol. 11:1019-1028(1994).
RN [8]
RP CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, SUBUNIT, AND ACTIVATION
RP BY PROTEOLYSIS IN VITRO.
RX PubMed=5336022; DOI=10.1016/0003-9861(66)90025-7;
RA Williams F.R., Hager L.P.;
RT "Crystalline flavin pyruvate oxidase from Escherichia coli. I. Isolation
RT and properties of the flavoprotein.";
RL Arch. Biochem. Biophys. 116:168-176(1966).
RN [9]
RP ACTIVATION BY PROTEOLYSIS IN VITRO.
RC STRAIN=W;
RX PubMed=334770; DOI=10.1016/s0021-9258(17)41046-5;
RA Russell P., Hager L.P., Gennis R.B.;
RT "Characterization of the proteolytic activation of pyruvate oxidase.
RT Control by specific ligands and by the flavin oxidation-reduction state.";
RL J. Biol. Chem. 252:7877-7882(1977).
RN [10]
RP ACTIVITY REGULATION, ACTIVATION BY PROTEOLYSIS IN VITRO, AND LIPID-BINDING.
RC STRAIN=W;
RX PubMed=334771; DOI=10.1016/s0021-9258(17)41047-7;
RA Russell P., Schrock H.L., Gennis R.B.;
RT "Lipid activation and protease activation of pyruvate oxidase. Evidence
RT suggesting a common site of interaction on the protein.";
RL J. Biol. Chem. 252:7883-7887(1977).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=B;
RX PubMed=365232; DOI=10.1021/bi00619a004;
RA Shaw-Goldstein L.A., Gennis R.B., Walsh C.;
RT "Identification, localization, and function of the thiamin pyrophosphate
RT and flavin adenine dinucleotide dependent pyruvate oxidase in isolated
RT membrane vesicles of Escherichia coli B.";
RL Biochemistry 17:5605-5613(1978).
RN [12]
RP CATALYTIC ACTIVITY, ENZYME KINETICS, METAL COFACTOR, AND THIAMINE
RP DIPHOSPHATE COFACTOR.
RX PubMed=6286628; DOI=10.1016/s0021-9258(18)34115-2;
RA Blake R. II, O'Brien T.A., Gennis R.B., Hager L.P.;
RT "Role of the divalent metal cation in the pyruvate oxidase reaction.";
RL J. Biol. Chem. 257:9605-9611(1982).
RN [13]
RP CATALYTIC ACTIVITY, SUBUNIT, AND FAD COFACTOR.
RX PubMed=6752142; DOI=10.1016/s0021-9258(18)33597-x;
RA Recny M.A., Hager L.P.;
RT "Reconstitution of native Escherichia coli pyruvate oxidase from apoenzyme
RT monomers and FAD.";
RL J. Biol. Chem. 257:12878-12886(1982).
RN [14]
RP ACTIVITY REGULATION.
RX PubMed=6385860; DOI=10.1016/0003-9861(84)90506-x;
RA Kiuchi K., Hager L.P.;
RT "Reconstitution of the lipid-depleted pyruvate oxidase system of
RT Escherichia coli: the palmitic acid effect.";
RL Arch. Biochem. Biophys. 233:776-784(1984).
RN [15]
RP CATALYTIC ACTIVITY, PROTEOLYTIC CLEAVAGE IS NOT RELEVANT IN VIVO, AND
RP MUTAGENESIS OF 549-TYR--ARG-570.
RX PubMed=3527254; DOI=10.1021/bi00361a003;
RA Grabau C., Cronan J.E. Jr.;
RT "In vivo function of Escherichia coli pyruvate oxidase specifically
RT requires a functional lipid binding site.";
RL Biochemistry 25:3748-3751(1986).
RN [16]
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 [17]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16080684; DOI=10.1021/bp050073s;
RA Dittrich C.R., Bennett G.N., San K.Y.;
RT "Characterization of the acetate-producing pathways in Escherichia coli.";
RL Biotechnol. Prog. 21:1062-1067(2005).
RN [18] {ECO:0007744|PDB:3EY9, ECO:0007744|PDB:3EYA}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH FAD; MAGNESIUM AND
RP THIAMINE PYROPHOSPHATE, X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-549 IN
RP COMPLEX WITH FAD; MAGNESIUM AND THIAMINE PYROPHOSPHATE, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND DOMAIN.
RX PubMed=18988747; DOI=10.1073/pnas.0805027105;
RA Neumann P., Weidner A., Pech A., Stubbs M.T., Tittmann K.;
RT "Structural basis for membrane binding and catalytic activation of the
RT peripheral membrane enzyme pyruvate oxidase from Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:17390-17395(2008).
CC -!- FUNCTION: A peripheral cell membrane enzyme that catalyzes the
CC oxidative decarboxylation of pyruvate to form acetate and CO(2). It
CC channels electrons from the cytoplasm to the respiratory chain at the
CC cell membrane via ubiquinone (By similarity) (PubMed:18988747,
CC PubMed:2663858, PubMed:365232). The main pathway for acetate production
CC during stationary phase (PubMed:16080684). {ECO:0000255|HAMAP-
CC Rule:MF_00850, ECO:0000269|PubMed:16080684,
CC ECO:0000269|PubMed:18988747, ECO:0000269|PubMed:2663858,
CC ECO:0000269|PubMed:365232}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + H2O + pyruvate = a ubiquinol + acetate + CO2;
CC Xref=Rhea:RHEA:27405, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:16389,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:17976, ChEBI:CHEBI:30089; EC=1.2.5.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00850,
CC ECO:0000269|PubMed:18988747, ECO:0000269|PubMed:2663858,
CC ECO:0000269|PubMed:3527254, ECO:0000269|PubMed:365232,
CC ECO:0000269|PubMed:6286628, ECO:0000269|PubMed:6752142,
CC ECO:0000305|PubMed:5336022};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00850,
CC ECO:0000269|PubMed:5336022, ECO:0000269|PubMed:6752142};
CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_00850,
CC ECO:0000269|PubMed:6752142};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00850,
CC ECO:0000269|PubMed:5336022, ECO:0000269|PubMed:6286628,
CC ECO:0000269|PubMed:6752142};
CC Note=Binds 1 Mg(2+) ion per subunit; Mn(2+) is also functional. The
CC Me2+-thiamine diphosphate complex is the true cofactor.
CC {ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:6286628,
CC ECO:0000269|PubMed:6752142};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00850,
CC ECO:0000269|PubMed:18988747, ECO:0000269|PubMed:5336022,
CC ECO:0000269|PubMed:6286628};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00850, ECO:0000269|PubMed:18988747,
CC ECO:0000269|PubMed:6286628};
CC -!- ACTIVITY REGULATION: The C-terminus inhibits activity; it has to move
CC for the enzyme to be active (PubMed:18988747). Activated by lipid-
CC binding, which occurs via the C-terminus; detergents also activate the
CC enzyme (PubMed:334770, PubMed:334771, PubMed:2663858, PubMed:18988747).
CC Specifically activated by palmitic acid; 12 (lauric) and 14-carbon
CC (myristic) fatty acids as well as unsaturated 16 and 18-carbon fatty
CC acids also activate the enzyme (PubMed:6385860). Lipid affinity is
CC increased in the presence of pyruvate plus the thiamine pyrophosphate
CC cofactor (PubMed:334770, PubMed:334771, PubMed:2663858,
CC PubMed:18988747). {ECO:0000255|HAMAP-Rule:MF_00850,
CC ECO:0000269|PubMed:18988747, ECO:0000269|PubMed:2663858,
CC ECO:0000269|PubMed:334770, ECO:0000269|PubMed:334771,
CC ECO:0000269|PubMed:6385860}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=90 mM for pyruvate, non-activated form
CC {ECO:0000269|PubMed:18988747};
CC KM=12 mM for pyruvate, activated form {ECO:0000269|PubMed:18988747};
CC Note=kcat is 7 sec(-1) for non-activated, 200 sec(-1) for activated
CC form. {ECO:0000269|PubMed:18988747};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00850,
CC ECO:0000269|PubMed:18988747, ECO:0000269|PubMed:6752142,
CC ECO:0000305|PubMed:5336022}.
CC -!- INTERACTION:
CC P07003; P07003: poxB; NbExp=3; IntAct=EBI-909338, EBI-909338;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00850, ECO:0000269|PubMed:365232, ECO:0000305|PubMed:5336022};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00850,
CC ECO:0000269|PubMed:365232, ECO:0000305|PubMed:5336022}; Cytoplasmic
CC side {ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:365232}.
CC -!- INDUCTION: Activity is maximal in late exponential and early stationary
CC phase (at protein level) (PubMed:8022274, PubMed:16080684). Expression
CC increases at pH 6.0 (PubMed:16080684). Under control of rpoS (at
CC protein level). Transcribed at lower levels during anaerobic growth
CC (PubMed:8022274). {ECO:0000269|PubMed:16080684,
CC ECO:0000269|PubMed:8022274}.
CC -!- DOMAIN: Has 4 domains; the Pyr domain which binds the pyrimidine moiety
CC of the thiamine pyrophosphate cofactor, the FAD-binding domain, the PP-
CC binding domain which binds the pyrophosphate portion of thiamine
CC pyrophosphate and the C-terminal membrane binding region, which
CC includes the in vitro-derived alpha-peptide (residues 550-572). The C-
CC terminus is held closely against the rest of the protein and covers the
CC active site; during activation it detaches from the rest of the protein
CC and folds into an amphipathic helix upon membrane binding. Comparison
CC of full-length and proteolyzed structures shows activation is a result
CC of conformational changes that expose the active site.
CC {ECO:0000269|PubMed:18988747}.
CC -!- PTM: Activated by limited proteolytic digestion in vitro. This cleavage
CC produces a peptide (alpha-peptide) and mimics the activation of enzyme
CC by phospholipids (PubMed:5336022, PubMed:3902830, PubMed:334770,
CC PubMed:334771). Protease activation and lipid-activation are mutually
CC exclusive. Proteolytic cleavage results in the loss of the high
CC affinity lipid-binding site of the enzyme; the cleaved protein is no
CC longer activated by lipids or detergents (PubMed:334771,
CC PubMed:2663858). The proteolytically cleaved enzyme does not represent
CC a functional cleavage in vivo (PubMed:3527254).
CC {ECO:0000269|PubMed:2663858, ECO:0000269|PubMed:334770,
CC ECO:0000269|PubMed:334771, ECO:0000269|PubMed:3527254,
CC ECO:0000269|PubMed:3902830, ECO:0000269|PubMed:5336022}.
CC -!- DISRUPTION PHENOTYPE: Not essential it can be deleted.
CC {ECO:0000269|PubMed:16080684}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000255|HAMAP-
CC Rule:MF_00850}.
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DR EMBL; X04105; CAA27725.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73958.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35585.1; -; Genomic_DNA.
DR EMBL; S73268; AAB31180.1; -; Genomic_DNA.
DR EMBL; M28208; AAB59101.1; -; Genomic_DNA.
DR EMBL; L47688; AAB59102.1; -; Genomic_DNA.
DR EMBL; L47689; AAB59103.1; -; Genomic_DNA.
DR EMBL; L47690; AAB59104.1; -; Genomic_DNA.
DR EMBL; L47691; AAB59105.1; -; Genomic_DNA.
DR EMBL; L47692; AAB59106.1; -; Genomic_DNA.
DR EMBL; L47693; AAB59107.1; -; Genomic_DNA.
DR EMBL; L47694; AAB59108.1; -; Genomic_DNA.
DR EMBL; L47695; AAB59109.1; -; Genomic_DNA.
DR PIR; A23648; DEECPC.
DR RefSeq; NP_415392.1; NC_000913.3.
DR RefSeq; WP_000815337.1; NZ_SSZK01000002.1.
DR PDB; 3EY9; X-ray; 2.90 A; A/B=1-572.
DR PDB; 3EYA; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-549.
DR PDBsum; 3EY9; -.
DR PDBsum; 3EYA; -.
DR AlphaFoldDB; P07003; -.
DR SMR; P07003; -.
DR BioGRID; 4262101; 20.
DR BioGRID; 850492; 1.
DR DIP; DIP-36216N; -.
DR IntAct; P07003; 4.
DR STRING; 511145.b0871; -.
DR ChEMBL; CHEMBL3380; -.
DR SWISS-2DPAGE; P07003; -.
DR jPOST; P07003; -.
DR PaxDb; P07003; -.
DR PRIDE; P07003; -.
DR EnsemblBacteria; AAC73958; AAC73958; b0871.
DR EnsemblBacteria; BAA35585; BAA35585; BAA35585.
DR GeneID; 946132; -.
DR KEGG; ecj:JW0855; -.
DR KEGG; eco:b0871; -.
DR PATRIC; fig|1411691.4.peg.1406; -.
DR EchoBASE; EB0747; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_6; -.
DR InParanoid; P07003; -.
DR OMA; YEATHEC; -.
DR PhylomeDB; P07003; -.
DR BioCyc; EcoCyc:PYRUVOXID-MON; -.
DR BioCyc; MetaCyc:PYRUVOXID-MON; -.
DR BRENDA; 1.2.5.1; 2026.
DR EvolutionaryTrace; P07003; -.
DR PRO; PR:P07003; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0008289; F:lipid binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0052737; F:pyruvate dehydrogenase (quinone) activity; IDA:EcoCyc.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:EcoCyc.
DR GO; GO:0048039; F:ubiquinone binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042867; P:pyruvate catabolic process; IMP:EcoCyc.
DR GO; GO:0006090; P:pyruvate metabolic process; IMP:EcoCyc.
DR HAMAP; MF_00850; POX; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR044261; PoxB-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; FAD; Flavoprotein; Lipid-binding; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Oxidoreductase; Pyruvate;
KW Reference proteome; Thiamine pyrophosphate; Ubiquinone.
FT CHAIN 1..572
FT /note="Pyruvate dehydrogenase [ubiquinone]"
FT /id="PRO_0000044606"
FT REGION 1..182
FT /note="Pyr domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00850,
FT ECO:0000269|PubMed:18988747"
FT REGION 183..334
FT /note="FAD-binding domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00850,
FT ECO:0000269|PubMed:18988747"
FT REGION 335..530
FT /note="PP-binding domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00850,
FT ECO:0000269|PubMed:18988747"
FT REGION 531..572
FT /note="Membrane-binding domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00850,
FT ECO:0000269|PubMed:18988747"
FT BINDING 50
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00850,
FT ECO:0000269|PubMed:18988747, ECO:0007744|PDB:3EY9,
FT ECO:0007744|PDB:3EYA"
FT BINDING 210
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18988747,
FT ECO:0007744|PDB:3EY9, ECO:0007744|PDB:3EYA"
FT BINDING 234..235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18988747,
FT ECO:0007744|PDB:3EY9, ECO:0007744|PDB:3EYA"
FT BINDING 251..254
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00850,
FT ECO:0000269|PubMed:18988747, ECO:0007744|PDB:3EY9,
FT ECO:0007744|PDB:3EYA"
FT BINDING 274..278
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00850,
FT ECO:0000269|PubMed:18988747, ECO:0007744|PDB:3EY9,
FT ECO:0007744|PDB:3EYA"
FT BINDING 292
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00850,
FT ECO:0000269|PubMed:18988747, ECO:0007744|PDB:3EY9,
FT ECO:0007744|PDB:3EYA"
FT BINDING 297
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18988747,
FT ECO:0007744|PDB:3EY9, ECO:0007744|PDB:3EYA"
FT BINDING 311..312
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18988747,
FT ECO:0007744|PDB:3EY9, ECO:0007744|PDB:3EYA"
FT BINDING 382
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:18988747,
FT ECO:0007744|PDB:3EY9, ECO:0007744|PDB:3EYA"
FT BINDING 403..404
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18988747,
FT ECO:0007744|PDB:3EY9, ECO:0007744|PDB:3EYA"
FT BINDING 406..408
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00850,
FT ECO:0000269|PubMed:18988747, ECO:0007744|PDB:3EY9,
FT ECO:0007744|PDB:3EYA"
FT BINDING 433..435
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00850,
FT ECO:0000269|PubMed:18988747, ECO:0007744|PDB:3EY9,
FT ECO:0007744|PDB:3EYA"
FT BINDING 433
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00850,
FT ECO:0000269|PubMed:18988747, ECO:0007744|PDB:3EY9,
FT ECO:0007744|PDB:3EYA"
FT BINDING 460..466
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00850,
FT ECO:0000269|PubMed:18988747, ECO:0007744|PDB:3EY9,
FT ECO:0007744|PDB:3EYA"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00850,
FT ECO:0000269|PubMed:18988747, ECO:0007744|PDB:3EY9,
FT ECO:0007744|PDB:3EYA"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18988747,
FT ECO:0007744|PDB:3EY9, ECO:0007744|PDB:3EYA"
FT SITE 465
FT /note="Moves into active site upon enzyme activation, plays
FT a role in electron transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00850,
FT ECO:0000269|PubMed:18988747"
FT SITE 549..550
FT /note="In vitro cleavage to yield alpha-peptide"
FT /evidence="ECO:0000269|PubMed:3902830"
FT MUTAGEN 533
FT /note="A->T: In poxB11; poor activity in vivo, no longer
FT activated by lipids."
FT /evidence="ECO:0000269|PubMed:2663858"
FT MUTAGEN 549..572
FT /note="Missing: In poxB6. Inactive in vivo, does not
FT complement inactive mutants. Active in vitro, no longer
FT activated by nor binds to, detergents."
FT /evidence="ECO:0000269|PubMed:2663858,
FT ECO:0000269|PubMed:5336022"
FT MUTAGEN 553
FT /note="A->V: In poxB14; poor activity in vivo, no longer
FT activated by lipids."
FT /evidence="ECO:0000269|PubMed:2663858"
FT MUTAGEN 560
FT /note="D->P: In poxB15; normal activity."
FT /evidence="ECO:0000269|PubMed:2663858"
FT MUTAGEN 564..572
FT /note="Missing: In poxB7 Inactive in vivo, reduced activity
FT in vitro."
FT /evidence="ECO:0000269|PubMed:2663858"
FT MUTAGEN 564
FT /note="E->P: In poxB16; loss of activity, weakly activated
FT by cleavage."
FT /evidence="ECO:0000269|PubMed:2663858"
FT MUTAGEN 570..572
FT /note="Missing: In poxB8; reduced activity in vitro, not
FT activated by lipids."
FT /evidence="ECO:0000269|PubMed:2663858"
FT MUTAGEN 572
FT /note="R->G: In poxB10; reduced activity in vivo and in
FT vitro; may interact less with membranes."
FT /evidence="ECO:0000269|PubMed:2663858"
FT CONFLICT 364..365
FT /note="QQ -> HE (in Ref. 5; AAB59101/AAB59102)"
FT /evidence="ECO:0000305"
FT CONFLICT 414..416
FT /note="QAL -> HGV (in Ref. 5; AAB59101/AAB59102)"
FT /evidence="ECO:0000305"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 50..64
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:3EYA"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:3EY9"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 188..199
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:3EY9"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 284..293
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 312..319
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 330..348
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:3EY9"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:3EY9"
FT HELIX 359..369
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 382..390
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:3EYA"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 411..421
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 433..438
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 443..448
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 454..459
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:3EY9"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:3EY9"
FT TURN 478..480
FT /evidence="ECO:0007829|PDB:3EY9"
FT HELIX 487..493
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 496..501
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 507..516
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:3EYA"
FT STRAND 521..527
FT /evidence="ECO:0007829|PDB:3EYA"
FT HELIX 536..542
FT /evidence="ECO:0007829|PDB:3EY9"
FT TURN 543..545
FT /evidence="ECO:0007829|PDB:3EY9"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:3EY9"
FT STRAND 551..555
FT /evidence="ECO:0007829|PDB:3EY9"
FT STRAND 559..564
FT /evidence="ECO:0007829|PDB:3EY9"
SQ SEQUENCE 572 AA; 62011 MW; 57B38B9E3A92BDEA CRC64;
MKQTVAAYIA KTLESAGVKR IWGVTGDSLN GLSDSLNRMG TIEWMSTRHE EVAAFAAGAE
AQLSGELAVC AGSCGPGNLH LINGLFDCHR NHVPVLAIAA HIPSSEIGSG YFQETHPQEL
FRECSHYCEL VSSPEQIPQV LAIAMRKAVL NRGVSVVVLP GDVALKPAPE GATMHWYHAP
QPVVTPEEEE LRKLAQLLRY SSNIALMCGS GCAGAHKELV EFAGKIKAPI VHALRGKEHV
EYDNPYDVGM TGLIGFSSGF HTMMNADTLV LLGTQFPYRA FYPTDAKIIQ IDINPASIGA
HSKVDMALVG DIKSTLRALL PLVEEKADRK FLDKALEDYR DARKGLDDLA KPSEKAIHPQ
YLAQQISHFA ADDAIFTCDV GTPTVWAARY LKMNGKRRLL GSFNHGSMAN AMPQALGAQA
TEPERQVVAM CGDGGFSMLM GDFLSVVQMK LPVKIVVFNN SVLGFVAMEM KAGGYLTDGT
ELHDTNFARI AEACGITGIR VEKASEVDEA LQRAFSIDGP VLVDVVVAKE ELAIPPQIKL
EQAKGFSLYM LRAIISGRGD EVIELAKTNW LR
