ID A0A263NLH8_9PSED Unreviewed; 574 AA. AC A0A263NLH8; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 03-MAY-2023, entry version 15. 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=B7453_26825 {ECO:0000313|EMBL:OZO01464.1}; OS Pseudomonas sp. IB20. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1702250 {ECO:0000313|EMBL:OZO01464.1, ECO:0000313|Proteomes:UP000215734}; RN [1] {ECO:0000313|EMBL:OZO01464.1, ECO:0000313|Proteomes:UP000215734} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IB20 {ECO:0000313|EMBL:OZO01464.1, RC ECO:0000313|Proteomes:UP000215734}; RA Lira F., Olivares Pacheco J.A.; RT "Antartic Pseudomonas sp. IB20 genome sequencing and assembly."; RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases. 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:OZO01464.1}. 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; NMRE01000123; OZO01464.1; -; Genomic_DNA. DR AlphaFoldDB; A0A263NLH8; -. DR EnsemblBacteria; OZO01464; OZO01464; B7453_26825. DR OrthoDB; 9785953at2; -. DR Proteomes; UP000215734; 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 CDD; cd02014; TPP_POX; 1. DR CDD; cd07039; TPP_PYR_POX; 1. DR Gene3D; 3.40.50.970; -; 2. DR Gene3D; 3.40.50.1220; TPP-binding domain; 1. DR HAMAP; MF_00850; POX; 1. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR047211; POXB-like. DR InterPro; IPR044261; Pyruvate_dehydrogenase. 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_TPP-bd. DR InterPro; IPR047212; TPP_POXB-like. DR InterPro; IPR047210; TPP_PYR_POXB-like. DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1. DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1. DR Pfam; PF02775; TPP_enzyme_C; 1. DR Pfam; PF00205; TPP_enzyme_M; 1. DR Pfam; PF02776; TPP_enzyme_N; 1. DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 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|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:OZO01464.1}; KW Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_00850, KW ECO:0000256|RuleBase:RU362132}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_00850}. FT DOMAIN 5..171 FT /note="Thiamine pyrophosphate enzyme N-terminal TPP- FT binding" FT /evidence="ECO:0000259|Pfam:PF02776" FT DOMAIN 192..319 FT /note="Thiamine pyrophosphate enzyme central" FT /evidence="ECO:0000259|Pfam:PF00205" FT DOMAIN 381..527 FT /note="Thiamine pyrophosphate enzyme TPP-binding" FT /evidence="ECO:0000259|Pfam:PF02775" FT REGION 183..334 FT /note="FAD-binding domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT REGION 533..574 FT /note="Membrane-binding domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 51 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 251..254 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 274..278 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 292 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 408..410 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 435..437 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 435 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 462..468 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT BINDING 462 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850" FT SITE 467 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 574 AA; 62305 MW; 644C2C5023C2BF57 CRC64; MAKINLAQQL ATTLEQAGIK RIWGLTGDSL NGLTDALRTM DSIEWMHVRH EEVAAFAAGA EAAATGELTV CAGSCGPGNL HLINGLFDCH RNHVPVLAIA AQIPSSEIGL NYFQETHPQE LFKECSHFIE LVTNPEQMPQ VLHRAMRSAI LNRGVAVVVI PGDVSLLEVE DKLKPWPALH APRTLPAEQD LQRLTEILQS SQKVTLLCGS GCAGAHDQVV ALADALGAPV VHALRGKEHV EWDNPFDVGM TGLIGFSSGY HAMLNCDTLI MLGTDFPYRQ FYPTDAKIIQ VDRNPQALGR RATLDLGIAA DVSETLDALL PRLTRKADRS FLDTSLKHYE KARQGLDDLA QPSKPDRPIH PQYVARLLSE LADDDAIFTA DVGSPTVWAA RYLKMNGKRR LIGSFNHGSM ANAMPQAIGA QAAFPGRQVI SMSGDGGFAM LMGDFISLAQ LKLPVKVIVF DNSSLGFVAM EMKAAGYLDT GTELKNPDFA AMSNAMGILG IRVEQSEDLE PALRRALAHD GPVLVDVVTA TQELVMPPTI KLEQAKGFSL YMLKAVMSGR GDEVIELART NWLR //