ODPA_DICDI
ID ODPA_DICDI Reviewed; 377 AA.
AC Q54C70;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=pdhA; ORFNames=DDB_G0292994;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
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) (By similarity). {ECO:0000250}.
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; AAFI02000199; EAL60849.1; -; Genomic_DNA.
DR RefSeq; XP_629349.1; XM_629347.1.
DR AlphaFoldDB; Q54C70; -.
DR SMR; Q54C70; -.
DR STRING; 44689.DDB0230193; -.
DR PaxDb; Q54C70; -.
DR EnsemblProtists; EAL60849; EAL60849; DDB_G0292994.
DR GeneID; 8629073; -.
DR KEGG; ddi:DDB_G0292994; -.
DR dictyBase; DDB_G0292994; pdhA.
DR eggNOG; KOG0225; Eukaryota.
DR HOGENOM; CLU_029393_5_2_1; -.
DR InParanoid; Q54C70; -.
DR OMA; LGYEMPC; -.
DR PhylomeDB; Q54C70; -.
DR Reactome; R-DDI-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-DDI-70268; Pyruvate metabolism.
DR PRO; PR:Q54C70; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; ISS:dictyBase.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; ISS:dictyBase.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISS:dictyBase.
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; Pyruvate; Reference proteome;
KW Thiamine pyrophosphate; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..377
FT /note="Pyruvate dehydrogenase E1 component subunit alpha,
FT mitochondrial"
FT /id="PRO_0000327983"
SQ SEQUENCE 377 AA; 41988 MW; BD3481894B7348C3 CRC64;
MLSNFLKVNS KALGHIRTFA SKSGEIKHNF KKADTYLCDG PSDSTVTNKD ELISFFTEMS
RFRRLETVCD GLYKKKLIRG FCHLYTGQEA VCAGLESAIT KDDHIITAYR DHTYMLSRGA
TPEEIFAELL MKETGCSKGK GGSMHMFTKN FYGGNGIVGA QCPLGAGIAF AQKYNKTGNV
CLAMYGDGAA NQGQLFEAFN MASLWKLPVI FICENNKYGM GTSQKRSTAG HDFYTRGHYV
AGLKVDGMDV FAVKEAGKYA AEWCRAGNGP IILEMDTYRY VGHSMSDPGI TYRTREEVNH
VRQTRDPIEN IRQIILDNKI ATEDQLAAIE ETVRDEMEKA SEKAIAAPLP QARELFTNVY
LQEVPVRGVE FVNSFKP
