ID A0A358GHM9_PAESP Unreviewed; 575 AA. AC A0A358GHM9; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 12-OCT-2022, entry version 12. DE RecName: Full=Pyruvate dehydrogenase [ubiquinone] {ECO:0000256|HAMAP-Rule:MF_00850}; DE EC=1.2.5.1 {ECO:0000256|HAMAP-Rule:MF_00850}; DE AltName: Full=Pyruvate oxidase {ECO:0000256|HAMAP-Rule:MF_00850}; DE Short=POX {ECO:0000256|HAMAP-Rule:MF_00850}; DE AltName: Full=Pyruvate:ubiquinone-8 oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00850}; GN Name=poxB {ECO:0000256|HAMAP-Rule:MF_00850}; GN ORFNames=DEF35_12105 {ECO:0000313|EMBL:HBU82368.1}; OS Paenibacillus sp. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus. OX NCBI_TaxID=58172 {ECO:0000313|EMBL:HBU82368.1, ECO:0000313|Proteomes:UP000261894}; RN [1] {ECO:0000313|EMBL:HBU82368.1, ECO:0000313|Proteomes:UP000261894} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA10718 {ECO:0000313|EMBL:HBU82368.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). 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. {ECO:0000256|HAMAP-Rule:MF_00850}. 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:0000256|HAMAP-Rule:MF_00850}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00850}; CC Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_00850}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00850}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00850}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00850}; CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00850}; CC -!- ACTIVITY REGULATION: The C-terminus inhibits activity; it has to move CC for the enzyme to be active. Activated by lipid-binding, which occurs CC via the C-terminus. {ECO:0000256|HAMAP-Rule:MF_00850}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00850}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00850}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00850}; CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00850}. 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. The C- CC terminus is held closely against the rest of the protein and covers the CC active site; during activation it unfolds from the rest of the protein CC and forms an amphipathic helix upon membrane binding, exposing the CC active site. {ECO:0000256|HAMAP-Rule:MF_00850}. CC -!- SIMILARITY: Belongs to the TPP enzyme family. CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|HAMAP-Rule:MF_00850, CC ECO:0000256|RuleBase:RU362132}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00850}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HBU82368.1}. 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; DOOE01000018; HBU82368.1; -; Genomic_DNA. DR EnsemblBacteria; HBU82368; HBU82368; DEF35_12105. DR Proteomes; UP000261894; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0052737; F:pyruvate dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule. DR GO; GO:0048039; F:ubiquinone binding; IEA:UniProtKB-UniRule. DR GO; GO:0042867; P:pyruvate catabolic process; IEA:UniProtKB-UniRule. 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 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00850}; KW FAD {ECO:0000256|HAMAP-Rule:MF_00850}; KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00850}; KW Lipid-binding {ECO:0000256|HAMAP-Rule:MF_00850}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00850}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00850}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00850}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00850}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00850}; KW Pyruvate {ECO:0000256|HAMAP-Rule:MF_00850, ECO:0000313|EMBL:HBU82368.1}; KW Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_00850, KW ECO:0000256|RuleBase:RU362132}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_00850, ECO:0000313|EMBL:HBU82368.1}. FT DOMAIN 4..168 FT /note="TPP_enzyme_N" FT /evidence="ECO:0000259|Pfam:PF02776" FT DOMAIN 193..320 FT /note="TPP_enzyme_M" FT /evidence="ECO:0000259|Pfam:PF00205" FT DOMAIN 382..528 FT /note="TPP_enzyme_C" FT /evidence="ECO:0000259|Pfam:PF02775" FT REGION 184..335 FT /note="FAD-binding domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT REGION 534..575 FT /note="Membrane-binding domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 50 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 252..255 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 275..279 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 293 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 409..411 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 436..438 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 436 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 463..469 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 463 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT SITE 468 FT /note="Moves into active site upon enzyme activation, plays FT a role in electron transfer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" SQ SEQUENCE 575 AA; 62614 MW; 99CDB7A34000433A CRC64; MKKTIADVLV EALLNAGIKR IYGIVGDSLN AVLDSIRRSG KIEWIHVRHE EVAAFAAGAD AQVSGSIAVC AGSSGPGNMH LINGLYDCHR NRVPVLAIAA HIPSDEIGSE YFQATHPEYL FQECSHYCEV ITTAKQMPRS FTMAMQTAVA RSGVSVIILP GDVAALEAAD LPVPEHVYHP THPVVHPSEP ELRKLAEFLN QGKKITLLCG AGCAGAREPL MQLCDRLKSP MVIALRGKEY LEYDNPYSVG LTGLIGYSSG YHAMMDCDVL LMLGTDFPYR QFFPEDAVVV QVDIQSSHLG RRTKLDYGVC GDVKATIEML LPYLTEEHSD KHLHKSVERY EKVRKELDEL AVGKPGKMPI HPQYLTKVIS DAAAENAIFT CDVGTPTVWA ARYIEMSRNR RLLGSFSHGT MANALPQAIG AQVSDPGRQV ISLSGDGGIA MLMGDLLTLK QHNLPIKVVV FNNGALGFVE LEMKAAGLLE SGTELVNPNF AMVAQAMGLE GIRVEDPADL EGAVERALLH DGPVLIDVVV NRQELSLPPK INIKQAEGFT LWMMKAVLNG RGDELIELAK TNLLR //