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Database: UniProt
Entry: A0A0D6PFP3_9PROT
LinkDB: A0A0D6PFP3_9PROT
Original site: A0A0D6PFP3_9PROT 
ID   A0A0D6PFP3_9PROT        Unreviewed;       573 AA.
AC   A0A0D6PFP3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=Aam_053_014 {ECO:0000313|EMBL:GAN80580.1};
OS   Acidocella aminolytica 101 = DSM 11237.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidocella.
OX   NCBI_TaxID=1120923 {ECO:0000313|EMBL:GAN80580.1, ECO:0000313|Proteomes:UP000032668};
RN   [1] {ECO:0000313|EMBL:GAN80580.1, ECO:0000313|Proteomes:UP000032668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=101 / DSM 11237 {ECO:0000313|Proteomes:UP000032668};
RA   Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT   "Whole genome sequence of Acidocella aminolytica 101 = DSM 11237.";
RL   Submitted (NOV-2012) 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:GAN80580.1}.
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DR   EMBL; BANC01000052; GAN80580.1; -; Genomic_DNA.
DR   RefSeq; WP_048878988.1; NZ_FQVJ01000060.1.
DR   AlphaFoldDB; A0A0D6PFP3; -.
DR   STRING; 1120923.SAMN02746095_03742; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000032668; 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:GAN80580.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032668};
KW   Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_00850,
KW   ECO:0000256|RuleBase:RU362132};
KW   Ubiquinone {ECO:0000256|HAMAP-Rule:MF_00850}.
FT   DOMAIN          4..113
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          191..318
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          380..526
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          182..333
FT                   /note="FAD-binding domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00850"
FT   REGION          532..573
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         273..277
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00850"
FT   BINDING         291
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00850"
FT   BINDING         407..409
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00850"
FT   BINDING         434..436
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00850"
FT   BINDING         434
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00850"
FT   BINDING         461..467
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00850"
FT   BINDING         461
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00850"
FT   SITE            466
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   573 AA;  61220 MW;  3FB5F9269BE5EF13 CRC64;
     MQATAASYMA ATLAAAGVRR VYGVVGDSLN GFTDALREQG RIDWKHMRHE EGAAFAAGAE
     AQLTGRLAVC AGSCGPGNLH LINGLFDAHR SQAPVLAIAA HIPSTEIGID YFQATHPEIL
     FKECSHYCEL VSNPRQLPQI LERAIRAAVA SKGVAVVIIP GDVALGELKA AVPSFLLPEP
     PVVRPSDMVL EETATLLNGT NRTTILCGAG CEGAHDEVIA LAAKLQAPIV HALRGKEHVE
     HDNPYDVGMT GFIGFASGYK ALKSCDTLVM LGTGFPYRQF YPEAAKVVQI DIRPEALGNR
     CPLAKGLVGD VKETLKVLLP RLVQQNDESF LRAAVADYHE ARAELDELAK ITPASKHVHP
     QQLNRLVSEL AAPDAIFTCD VGTPTVWAAR YLRLGGGRRL LGSFNHGSMA NALLQAIGAQ
     AAFPQRQVVS LSGDGGFTMM MGDFLTLSQL QLPVKVIVLN NGTLGFVELE MKANGFLDTG
     VDLQNPDFAA MANAMGVKGV RVDKPQDLEA GLREVLAHPG PALLDVVSAR QELVMPPKTT
     AKDVKSFGLF LLKAVMNGRA SQVVDLTKVN LFR
//
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