ID W5C3E3_WHEAT Unreviewed; 420 AA.
AC W5C3E3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|RuleBase:RU361139};
DE EC=1.2.4.1 {ECO:0000256|RuleBase:RU361139};
GN ORFNames=CAMPLR22A2D_LOCUS100 {ECO:0000313|EMBL:SPT15511.1},
GN CFC21_027067 {ECO:0000313|EMBL:KAF7012923.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS2D02G010700.1};
RN [1] {ECO:0000313|EMBL:KAF7012923.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7012923.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS2D02G010700.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS2D02G010700.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EMBL:SPT15511.1, ECO:0000313|Proteomes:UP000280104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Thind KAUR A.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblPlants:TraesCS2D02G010700.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [5] {ECO:0000313|EMBL:KAF7012923.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7012923.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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; CM022216; KAF7012923.1; -; Genomic_DNA.
DR EMBL; LS480641; SPT15511.1; -; Genomic_DNA.
DR SMR; W5C3E3; -.
DR STRING; 4565.W5C3E3; -.
DR PaxDb; 4565-Traes_2DS_1966D084E-1; -.
DR EnsemblPlants; TraesCS2D02G010700.1; TraesCS2D02G010700.1; TraesCS2D02G010700.
DR Gramene; TraesCAD_scaffold_058644_01G000200.1; TraesCAD_scaffold_058644_01G000200.1; TraesCAD_scaffold_058644_01G000200.
DR Gramene; TraesCLE_scaffold_049138_01G000600.1; TraesCLE_scaffold_049138_01G000600.1; TraesCLE_scaffold_049138_01G000600.
DR Gramene; TraesCS2D02G010700.1; TraesCS2D02G010700.1; TraesCS2D02G010700.
DR Gramene; TraesCS2D03G0019300.2; TraesCS2D03G0019300.2.CDS; TraesCS2D03G0019300.
DR Gramene; TraesKAR2D01G0004930.1; cds.TraesKAR2D01G0004930.1; TraesKAR2D01G0004930.
DR Gramene; TraesPAR_scaffold_035972_01G000600.1; TraesPAR_scaffold_035972_01G000600.1; TraesPAR_scaffold_035972_01G000600.
DR Gramene; TraesRN2D0100021500.2; TraesRN2D0100021500.2; TraesRN2D0100021500.
DR Gramene; TraesROB_scaffold_046316_01G000600.1; TraesROB_scaffold_046316_01G000600.1; TraesROB_scaffold_046316_01G000600.
DR Gramene; TraesWEE_scaffold_036313_01G000600.1; TraesWEE_scaffold_036313_01G000600.1; TraesWEE_scaffold_036313_01G000600.
DR eggNOG; KOG0225; Eukaryota.
DR HOGENOM; CLU_029393_5_1_1; -.
DR OMA; WMYQKML; -.
DR Proteomes; UP000019116; Chromosome 2D.
DR Proteomes; UP000280104; Chromosome ii.
DR Proteomes; UP000815260; Chromosome 2D.
DR ExpressionAtlas; W5C3E3; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000019116};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139}.
FT DOMAIN 79..382
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT COILED 351..378
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 420 AA; 45927 MW; ADE202113C88FD88 CRC64;
MAAASFTAAK FLAPAAARSG GDRAPFPAPS AFSMRSLRHR PARRLSSVLA VSSDVLKAAP
AAAAYPAVTR EEALELYEDM ILGRNFEDMC AQMYYRGKMF GFVHLYNGQE AVSTGFIKQL
NQPDCVVSTY RDHVHALSKG VPARAVMAEL FGKATGCCRG QGGSMHMFSE PHNLLGGFAF
IGEGIPVATG AAFAAKYRHE VLKQSSPDGL DVTLAFFGDG TCNNGQFFEC LNMAQLWKLP
IIFVVENNLW AIGMSHLRST SDPEIWKKGP AFGMPGVHVD GMDVLKVREV AKEAIDRARR
GEGPTLVECE TYRFRGHSLA DPDELRRPDE KSHYAARDPI TSLKKYIIEQ NLASEAELKN
IEKKIDDVVE EAVEFADASP LPPRSQLLEN VFADPKGFGI GPDGKYRCED PKFTQGTAQV
//
