ID I1IVQ0_BRADI Unreviewed; 424 AA.
AC I1IVQ0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|RuleBase:RU361139};
DE EC=1.2.4.1 {ECO:0000256|RuleBase:RU361139};
GN Name=100843225 {ECO:0000313|EnsemblPlants:KQJ81560};
GN ORFNames=BRADI_5g01420v3 {ECO:0000313|EMBL:KQJ81560.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ81560.1};
RN [1] {ECO:0000313|EMBL:KQJ81560.1, ECO:0000313|EnsemblPlants:KQJ81560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ81560.1,
RC ECO:0000313|EnsemblPlants:KQJ81560};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ81560.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ81560.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ81560}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ81560};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC Evidence={ECO:0000256|RuleBase:RU361139};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU361139};
CC -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits.
CC {ECO:0000256|ARBA:ARBA00011130}.
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DR EMBL; CM000884; KQJ81560.1; -; Genomic_DNA.
DR RefSeq; XP_003580308.1; XM_003580260.3.
DR AlphaFoldDB; I1IVQ0; -.
DR STRING; 15368.I1IVQ0; -.
DR EnsemblPlants; KQJ81560; KQJ81560; BRADI_5g01420v3.
DR GeneID; 100843225; -.
DR Gramene; KQJ81560; KQJ81560; BRADI_5g01420v3.
DR KEGG; bdi:100843225; -.
DR eggNOG; KOG0225; Eukaryota.
DR HOGENOM; CLU_029393_5_1_1; -.
DR InParanoid; I1IVQ0; -.
DR OMA; WMYQKML; -.
DR OrthoDB; 166915at2759; -.
DR Proteomes; UP000008810; Chromosome 5.
DR ExpressionAtlas; I1IVQ0; baseline and differential.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:InterPro.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IBA:GO_Central.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR InterPro; IPR029061; THDP-binding.
DR NCBIfam; TIGR03182; PDH_E1_alph_y; 1.
DR PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361139};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU361139};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139}.
FT DOMAIN 83..386
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 424 AA; 45982 MW; C5A4866CC5134662 CRC64;
MAAASFTAAK FLAPVAARSG GDKAPSFPAA AAASMRPLRR RPAPRLSSVL AVSSDVLAGN
KAAPAAAAHP AVTREEALEL YEDMVLGRNF EDMCAQMYYR GKMFGFVHLY NGQEAVSTGF
IKLLNQPDCV VSTYRDHVHA LSKGVPARSV MAELFGKATG CCRGQGGSMH MFSEPHNLLG
GFAFIGEGIP VATGAAFAAK YRHEVLKQSG PDGLDVTLAF FGDGTCNNGQ FFECLNMAQL
WKLPIVFVVE NNLWAIGMSH LRATSDPEIW KKGPAFGMPG VHVDGMDVLK VREVAKEAID
RARRGEGPTL VECETYRFRG HSLADPDELR RPDEKSHYAA RDPITSLKKY IIEQNLASEA
ELKSIEKKID DVVEEAVEFA DASPLPPRSQ LLENVFADPK GFGIGPDGKY RCEDPKFTQG
TAQV
//
