ODPA_KLULA
ID ODPA_KLULA Reviewed; 412 AA.
AC O13366; Q6CKB5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial;
DE Short=PDHE1-A;
DE EC=1.2.4.1;
DE Flags: Precursor;
GN Name=PDA1; OrderedLocusNames=KLLA0F12001g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC MYA-539 / JBD100;
RX PubMed=9884236; DOI=10.1099/00221287-144-12-3437;
RA Zeeman A.-M., Luttik M.A.H., Thiele C., van Dijken J.P., Pronk J.T.,
RA Steensma H.Y.;
RT "Inactivation of the Kluyveromyces lactis KlPDA1 gene leads to loss of
RT pyruvate dehydrogenase activity, impairs growth on glucose and triggers
RT aerobic alcoholic fermentation.";
RL Microbiology 144:3437-3446(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + CO2; 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 -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: E1 activity is regulated by phosphorylation
CC (inactivation) and dephosphorylation (activation) of the alpha subunit.
CC {ECO:0000250}.
CC -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
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DR EMBL; AF023920; AAD03773.1; -; Genomic_DNA.
DR EMBL; CR382126; CAG98332.1; -; Genomic_DNA.
DR RefSeq; XP_455624.1; XM_455624.1.
DR AlphaFoldDB; O13366; -.
DR SMR; O13366; -.
DR STRING; 28985.XP_455624.1; -.
DR PRIDE; O13366; -.
DR EnsemblFungi; CAG98332; CAG98332; KLLA0_F12001g.
DR GeneID; 2894999; -.
DR KEGG; kla:KLLA0_F12001g; -.
DR eggNOG; KOG0225; Eukaryota.
DR HOGENOM; CLU_029393_5_2_1; -.
DR InParanoid; O13366; -.
DR OMA; LGYEMPC; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IEA:EnsemblFungi.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:EnsemblFungi.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0007124; P:pseudohyphal growth; IEA:EnsemblFungi.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR InterPro; IPR029061; THDP-binding.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1.
PE 3: Inferred from homology;
KW Glycolysis; Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate;
KW Reference proteome; Thiamine pyrophosphate; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..412
FT /note="Pyruvate dehydrogenase E1 component subunit alpha,
FT mitochondrial"
FT /id="PRO_0000020450"
FT CONFLICT 275..281
FT /note="YQASKFA -> TKL (in Ref. 1; AAD03773)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 45453 MW; CBCC8AB3DC4C7E96 CRC64;
MLSLKAQSSV VGKSSSLRLV RNFSKNVRAL SQVADETKPG DDDLVQIDLP ETSFEGYLLD
VPELSYQTTK SNLLQMYKDM IIVRRMEMAC DALYKAKKIR GFCHSSVGQE AIAVGIENAI
TKRDTVITSY RCHGFTYMRG AAVQAVLAEL MGRRTGVSFG KGGSMHLYAP GFYGGNGIVG
AQVPLGAGLA FAHQYKHEDA CSFALYGDGA SNQGQVFESF NMAKLWNLPA VFCCENNKYG
MGTAAARSSA MTEYFKRGQY IPGLKVNGMD ILAVYQASKF AKDWTVSGNG PIVLEYETYR
YGGHSMSDPG TTYRTRDEIQ HMRSKNDPIA GLKMHLLELG IATEDEIKAY DKAARKYVDE
QVELADAAPA PEAKMSILFE DVYVPGSETP TLRGRLQEDT WDFAKKSFAF RD
