ODPA_SCHPO
ID ODPA_SCHPO Reviewed; 409 AA.
AC Q10489;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
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; ORFNames=SPAC26F1.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; TYR-306; SER-310 AND
RP SER-312, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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; CU329670; CAA97360.1; -; Genomic_DNA.
DR PIR; T38417; T38417.
DR RefSeq; NP_594892.1; NM_001020321.2.
DR AlphaFoldDB; Q10489; -.
DR SMR; Q10489; -.
DR BioGRID; 278076; 6.
DR STRING; 4896.SPAC26F1.03.1; -.
DR iPTMnet; Q10489; -.
DR MaxQB; Q10489; -.
DR PaxDb; Q10489; -.
DR PRIDE; Q10489; -.
DR EnsemblFungi; SPAC26F1.03.1; SPAC26F1.03.1:pep; SPAC26F1.03.
DR GeneID; 2541579; -.
DR KEGG; spo:SPAC26F1.03; -.
DR PomBase; SPAC26F1.03; pda1.
DR VEuPathDB; FungiDB:SPAC26F1.03; -.
DR eggNOG; KOG0225; Eukaryota.
DR HOGENOM; CLU_029393_5_2_1; -.
DR InParanoid; Q10489; -.
DR OMA; LGYEMPC; -.
DR PhylomeDB; Q10489; -.
DR Reactome; R-SPO-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-SPO-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-SPO-5362517; Signaling by Retinoic Acid.
DR Reactome; R-SPO-70268; Pyruvate metabolism.
DR PRO; PR:Q10489; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; ISS:PomBase.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISS:PomBase.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
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 ?..409
FT /note="Pyruvate dehydrogenase E1 component subunit alpha,
FT mitochondrial"
FT /id="PRO_0000020451"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 306
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 409 AA; 45138 MW; 0FAE33765847C185 CRC64;
MFRTCTKIGT VPKVLVNQKG LIDGLRRVTT DATTSRANPA HVPEEHDKPF PVKLDDSVFE
GYKIDVPSTE IEVTKGELLG LYEKMVTIRR LELACDALYK AKKIRGFCHL SIGQEAVAAG
IEGAITLDDS IITSYRCHGF AYTRGLSIRS IIGELMGRQC GASKGKGGSM HIFAKNFYGG
NGIVGAQIPL GAGIGFAQKY LEKPTTTFAL YGDGASNQGQ AFEAFNMAKL WGLPVIFACE
NNKYGMGTSA ERSSAMTEFY KRGQYIPGLL VNGMDVLAVL QASKFAKKYT VENSQPLLME
FVTYRYGGHS MSDPGTTYRS REEVQKVRAA RDPIEGLKKH IMEWGVANAN ELKNIEKRIR
GMVDEEVRIA EESPFPDPIE ESLFSDVYVA GTEPAYARGR NSLEYHQYK
