ID L0M843_ENTBF Unreviewed; 572 AA.
AC L0M843;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 OrderedLocusNames=D782_2938 {ECO:0000313|EMBL:AGB78891.1};
OS Enterobacteriaceae bacterium (strain FGI 57).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=693444 {ECO:0000313|EMBL:AGB78891.1, ECO:0000313|Proteomes:UP000011002};
RN [1] {ECO:0000313|EMBL:AGB78891.1, ECO:0000313|Proteomes:UP000011002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI 57 {ECO:0000313|EMBL:AGB78891.1,
RC ECO:0000313|Proteomes:UP000011002};
RX PubMed=23469353; DOI=10.1128/genomeA.00238-12;
RA Aylward F.O., Tremmel D.M., Bruce D.C., Chain P., Chen A.,
RA Walston Davenport K., Detter C., Han C.S., Han J., Huntemann M.,
RA Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M.,
RA Pagani I., Pati A., Pitluck S., Deshpande S., Goodwin L., Woyke T.,
RA Currie C.R.;
RT "Complete genome of Enterobacteriaceae bacterium strain FGI 57, a strain
RT associated with leaf-cutter ant fungus gardens.";
RL Genome Announc. 1:E00238-12(2013).
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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00850}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00850}; 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}.
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DR EMBL; CP003938; AGB78891.1; -; Genomic_DNA.
DR AlphaFoldDB; L0M843; -.
DR STRING; 693444.D782_2938; -.
DR KEGG; ebf:D782_2938; -.
DR PATRIC; fig|693444.3.peg.2805; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_6; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000011002; Chromosome.
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:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 inner membrane {ECO:0000256|HAMAP-Rule:MF_00850};
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 Ligase {ECO:0000313|EMBL:AGB78891.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011002};
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..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 379..525
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 335..530
FT /note="PP-binding domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850"
FT REGION 531..572
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 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 406..408
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850"
FT BINDING 433..435
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850"
FT BINDING 433
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850"
FT BINDING 460..466
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00850"
FT SITE 465
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 572 AA; 62058 MW; E0E237F6D0DB693D CRC64;
MKQTVAAYIA KTLEQAGVKR IWGVTGDSLN GLSDSLNRMG TIDWMPTRHE EVAAFAAGAE
AQLTGELAVC AGSCGPGNLH LINGLFDCHR NHVPVLAIAA HIPSSEIGSG YFQETHPQEL
FRECSHYCEL VSSPEQIPQV LAIAMRKAVL NRGVSVVVLP GDVALKAAPE SASSHWYHAP
LPVVTPAEEE LDKLAQLLRY SSNIAFLCGS GCAGAHKELV EFAARLKAPI VHALRGKEHV
EYDNPYDVGM TGLIGFSSGF HAMMNADTLI LLGTQFPYRP FYPTDAKIIQ IDINPASIGA
HSKVDMALVG DIKSTLRALL PKLEEKTDRR FLDKALEHYR DARKGLDDLA KPSDKAIHPQ
YLAQQISHFA ADDAIFTCDV GTPTVWAARY LKMNGKRRLI GSFNHGSMAN AMPQALGAQA
THPGRQVVAM CGDGGFSMLM GDFLSVVQMK LPVKIFVFNN SVLGFVAMEM KAGGYLTDGT
ELHDTNFARI AEACGIPGIR VEKSADVDEA IQKAFSIDGP VLVDVVVAKE ELAMPPQIKL
EQAKGFSLYM LRAIINGRGD EVMELAKTNW LR
//
