ID   ODP2_BOVIN              Reviewed;          10 AA.
AC   P11180;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   11-DEC-2019, entry version 86.
DE   RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex;
DE            EC=2.3.1.12;
DE   AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex;
DE   AltName: Full=Pyruvate dehydrogenase complex component E2;
DE   Flags: Fragment;
GN   Name=DLAT;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   PROTEIN SEQUENCE, AND LIPOYLATION AT LYS-5.
RX   PubMed=3117054; DOI=10.1042/bj2450919;
RA   Bradford A.P., Howell S., Aitken A., James L.A., Yeaman S.J.;
RT   "Primary structure around the lipoate-attachment site on the E2 component
RT   of bovine heart pyruvate dehydrogenase complex.";
RL   Biochem. J. 245:919-922(1987).
RN   [2]
RP   SUBUNIT.
RX   PubMed=20361979; DOI=10.1016/j.jmb.2010.03.043;
RA   Vijayakrishnan S., Kelly S.M., Gilbert R.J., Callow P., Bhella D.,
RA   Forsyth T., Lindsay J.G., Byron O.;
RT   "Solution structure and characterisation of the human pyruvate
RT   dehydrogenase complex core assembly.";
RL   J. Mol. Biol. 399:71-93(2010).
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)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-
CC         N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83111; EC=2.3.1.12;
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC       Note=Binds 2 lipoyl cofactors covalently. {ECO:0000250};
CC   -!- SUBUNIT: Part of the multimeric pyruvate dehydrogenase complex that
CC       contains multiple copies of pyruvate dehydrogenase (subunits PDH1A and
CC       PDHB, E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide
CC       dehydrogenase (DLD, E3) (By similarity). These subunits are bound to an
CC       inner core composed of about 48 DLAT and 12 PDHX molecules
CC       (PubMed:20361979). Interacts with PDK2 and PDK3 (By similarity).
CC       Interacts with SIRT4 (By similarity). Interacts with PDHB (By
CC       similarity). {ECO:0000250|UniProtKB:P10515,
CC       ECO:0000269|PubMed:20361979}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Delipoylated at Lys-5 by SIRT4, delipoylation decreases the PHD
CC       complex activity. {ECO:0000250|UniProtKB:P10515}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
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DR   CORUM; P11180; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Acyltransferase; Carbohydrate metabolism; Direct protein sequencing;
KW   Glucose metabolism; Lipoyl; Mitochondrion; Reference proteome; Repeat;
KW   Transferase; Tricarboxylic acid cycle.
FT   CHAIN           <1..>10
FT                   /note="Dihydrolipoyllysine-residue acetyltransferase
FT                   component of pyruvate dehydrogenase complex"
FT                   /id="PRO_0000162297"
FT   MOD_RES         5
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000269|PubMed:3117054"
FT   NON_TER         1
FT   NON_TER         10
SQ   SEQUENCE   10 AA;  1066 MW;  889BECD1ADD33AB1 CRC64;
     VETDKATVGF