ID   ODPT_ASCSU              Reviewed;         391 AA.
AC   P26268;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha type II, mitochondrial;
DE            Short=PDHA2;
DE            Short=PDHE1-A;
DE            EC=1.2.4.1;
DE   Flags: Precursor; Fragment;
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).
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 PDHA2; it is reactivated by dephosphorylation.
CC   -!- SUBUNIT: Heterotetramer of two PDHA2 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; M76554; AAA29377.1; -; mRNA.
DR   AlphaFoldDB; P26268; -.
DR   SMR; P26268; -.
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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glucose metabolism; Mitochondrion; Oxidoreductase;
KW   Phosphoprotein; Pyruvate; Thiamine pyrophosphate; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT         <1..17
FT                   /note="Mitochondrion"
FT   CHAIN           18..391
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha
FT                   type II, mitochondrial"
FT                   /id="PRO_0000020438"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         291
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   391 AA;  43207 MW;  BA66E56C300FB8E7 CRC64;
     SNIFKGPTVG SSVVAMSARL ASTEATFQAK PFKLHKLDSG PDVNMHVTKE DALRYYTQMQ
     TIRRMETAAG NLYKEKKVRG FCHLYSGQEA CAVGMKAAME PGDAAITAYR CHGWTYLSGS
     PVAKVLCELT GRITGNVYGK GGSMHMYGEN FYGGNGIVGA QQPLGTGIAF AMKYKKQKNV
     CITLFGDGAT NQGQLYESMN MAKLWELPVL YVCENNGYGM GTSAARSSAS TDYYTRGDYV
     PGFWVDGMDV LAVRQAIRWG KEWCNAGKGP LMIEMATYRY GGHSMSDPGT SYRTREEIQE
     VRKTRDPITG FKDKIVTAGL VTEDELKEVD KEIRKEVDAA VKQAHTDKEA PVEMLLTDIY
     YNTPAQYVRC TTEDVLQQYV TSEEAFKALS K