ID A0A3B6KCV0_WHEAT Unreviewed; 391 AA.
AC A0A3B6KCV0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|RuleBase:RU364074};
DE EC=1.2.4.1 {ECO:0000256|RuleBase:RU364074};
GN ORFNames=CFC21_064052 {ECO:0000313|EMBL:KAF7056668.1};
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:TraesCS5A02G030800.1};
RN [1] {ECO:0000313|EMBL:KAF7056668.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7056668.1};
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:TraesCS5A02G030800.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS5A02G030800.1};
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|EnsemblPlants:TraesCS5A02G030800.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7056668.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7056668.1};
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 -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO2.
CC {ECO:0000256|RuleBase:RU364074}.
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|ARBA:ARBA00043719,
CC ECO:0000256|RuleBase:RU364074};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU364074};
CC -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits.
CC {ECO:0000256|ARBA:ARBA00011130}.
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DR EMBL; CM022223; KAF7056668.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6KCV0; -.
DR SMR; A0A3B6KCV0; -.
DR STRING; 4565.A0A3B6KCV0; -.
DR EnsemblPlants; TraesCS5A02G030800.1; TraesCS5A02G030800.1; TraesCS5A02G030800.
DR Gramene; TraesCS5A02G030800.1; TraesCS5A02G030800.1; TraesCS5A02G030800.
DR Gramene; TraesCS5A03G0076200.1; TraesCS5A03G0076200.1.CDS; TraesCS5A03G0076200.
DR Gramene; TraesKAR5A01G0020350.1; cds.TraesKAR5A01G0020350.1; TraesKAR5A01G0020350.
DR Gramene; TraesRN5A0100077800.1; TraesRN5A0100077800.1; TraesRN5A0100077800.
DR Gramene; TraesROB_scaffold_002176_01G000100.1; TraesROB_scaffold_002176_01G000100.1; TraesROB_scaffold_002176_01G000100.
DR Gramene; TraesWEE_scaffold_002846_01G000100.1; TraesWEE_scaffold_002846_01G000100.1; TraesWEE_scaffold_002846_01G000100.
DR OMA; HETNTHA; -.
DR OrthoDB; 5473567at2759; -.
DR Proteomes; UP000019116; Chromosome 5A.
DR Proteomes; UP000815260; Chromosome 5A.
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 CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR027110; PDHB.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR11624; DEHYDROGENASE RELATED; 1.
DR PANTHER; PTHR11624:SF96; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364074};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU364074};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU364074}.
FT DOMAIN 71..246
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 391 AA; 42224 MW; 66F882DFC830D9EA CRC64;
MAVAPSPQAT AAAAALSRHR SAAVPPVPRS VRVATAARRP GWTRARAGLV ARAVVAAKGE
LASSDTGGHE VLMFEALREA MIEEMTLDPT VCMIGEDVGD YGGSYKVSKG LSEMFGDLRV
LDTPIAENSF TGMGIGAAMQ GLRPVVEGMN MGFLLLAYNQ ISNNCGMLPY TSGGQFKIPI
VIRGPGGVGR QLGAEHSQRL ESYFQSIPGI QMVACSTPYN AKGLLKAAIR SDNPVVLFEH
VLLYNLKEKI PDEEYICSLE EAEMVRPGSQ LTILTYSRMR YHVMQAVKTL VNKGYDPEVI
DIRSLKPFDL HTIGNSIKKT HRVLIVEECM RTGGIGASLR SAIIDNFWDE LDARPVCLSS
QDVPTPYAAT LEDATVVQPA QIVAAVEEIC Q
//
