ID   ODPA_ASCSU              Reviewed;         396 AA.
AC   P26267;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha type I, mitochondrial;
DE            Short=PDHA1;
DE            Short=PDHE1-A;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1565136; DOI=10.1016/0166-6851(92)90198-s;
RA   Johnson K.R., Komuniecki R., Sun Y., Wheelock M.J.;
RT   "Characterization of cDNA clones for the alpha subunit of pyruvate
RT   dehydrogenase from Ascaris suum.";
RL   Mol. Biochem. Parasitol. 51:37-48(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 285-298, AND PHOSPHORYLATION AT SER-289 AND SER-296.
RX   PubMed=3198613; DOI=10.1016/s0021-9258(18)37394-0;
RA   Thissen J., Komuniecki R.;
RT   "Phosphorylation and inactivation of the pyruvate dehydrogenase from the
RT   anaerobic parasitic nematode, Ascaris suum. Stoichiometry and amino acid
RT   sequence around the phosphorylation sites.";
RL   J. Biol. Chem. 263:19092-19097(1988).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the
CC       glycolytic pathway to the tricarboxylic cycle.
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   -!- ACTIVITY REGULATION: Pyruvate dehydrogenase activity is inhibited by
CC       phosphorylation of PDHA1; it is reactivated by dephosphorylation.
CC   -!- SUBUNIT: Heterotetramer of two PDHA1 and two PDHB subunits. The
CC       heterotetramer interacts with DLAT, and is part of the multimeric
CC       pyruvate dehydrogenase complex that contains multiple copies of
CC       pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT,
CC       E2) and lipoamide dehydrogenase (DLD, E3) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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DR   EMBL; M76555; AAA29376.1; -; mRNA.
DR   PIR; A31963; A31963.
DR   PIR; A45608; A45608.
DR   AlphaFoldDB; P26267; -.
DR   SMR; P26267; -.
DR   iPTMnet; P26267; -.
DR   BioCyc; MetaCyc:MON-18299; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; 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   Carbohydrate metabolism; Direct protein sequencing; Glucose metabolism;
KW   Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate;
KW   Thiamine pyrophosphate; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT   CHAIN           26..396
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha
FT                   type I, mitochondrial"
FT                   /id="PRO_0000020437"
FT   MOD_RES         289
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:3198613"
FT   MOD_RES         296
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:3198613"
SQ   SEQUENCE   396 AA;  43771 MW;  60A810BB5B48B836 CRC64;
     MIFVFANIFK VPTVSPSVMA ISVRLASTEA TFQTKPFKLH KLDSGPDINV HVTKEDAVHY
     YTQMLTIRRM ESAAGNLYKE KKVRGFCHLY SGQEACAVGT KAAMDAGDAA VTAYRCHGWT
     YLSGSSVAKV LCELTGRITG NVYGKGGSMH MYGENFYGGN GIVGAQQPLG TGIAFAMKYR
     KEKNVCITMF GDGATNQGQL FESMNMAKLW DLPVLYVCEN NGYGMGTAAA RSSASTDYYT
     RGDYVPGIWV DGMDVLAVRQ AVRWAKEWCN AGKGPLMIEM ATYRYSGHSM SDPGTSYRTR
     EEVQEVRKTR DPITGFKDKI VTAGLVTEDE IKEIDKQVRK EIDAAVKQAH TDKESPVELM
     LTDIYYNTPA QYVRCTTDEV LQKYLTSEEA VKALAK