ODP2_MESAU
ID ODP2_MESAU Reviewed; 219 AA.
AC P86197;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial {ECO:0000250|UniProtKB:P08461};
DE EC=2.3.1.12;
DE AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000250|UniProtKB:P08461};
DE AltName: Full=Pyruvate dehydrogenase complex component E2 {ECO:0000250|UniProtKB:P08461};
DE Short=PDC-E2 {ECO:0000250|UniProtKB:P08461};
DE Short=PDCE2 {ECO:0000250|UniProtKB:P08461};
DE Flags: Fragments;
GN Name=DLAT {ECO:0000250|UniProtKB:P08461};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(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. {ECO:0000250}.
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 Evidence={ECO:0000250|UniProtKB:P08461};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000250|UniProtKB:P08461};
CC Note=Binds 1 lipoyl cofactor covalently.
CC {ECO:0000250|UniProtKB:P08461};
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). These subunits are bound to an inner core
CC composed of about 48 DLAT and 12 PDHX molecules. Interacts with PDK2
CC and PDK3. Interacts with SIRT4. Interacts with PDHB.
CC {ECO:0000250|UniProtKB:P10515}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P08461}.
CC -!- TISSUE SPECIFICITY: Detected at higher levels in cauda epididymal
CC spermatazoa than in caput epididymal spermatazoa (at protein level).
CC {ECO:0000269|PubMed:20400973}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000255}.
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DR AlphaFoldDB; P86197; -.
DR SMR; P86197; -.
DR STRING; 10036.XP_005069352.1; -.
DR PRIDE; P86197; -.
DR eggNOG; KOG0557; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase 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 Gene3D; 3.30.559.10; -; 1.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR PANTHER; PTHR23151; PTHR23151; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Carbohydrate metabolism; Glucose metabolism; Lipoyl;
KW Mitochondrion; Phosphoprotein; Reference proteome; Repeat; Transferase;
KW Tricarboxylic acid cycle.
FT CHAIN <1..219
FT /note="Dihydrolipoyllysine-residue acetyltransferase
FT component of pyruvate dehydrogenase complex, mitochondrial"
FT /id="PRO_0000394399"
FT DOMAIN <1..>17
FT /note="Lipoyl-binding 1"
FT /evidence="ECO:0000250|UniProtKB:P08461"
FT DOMAIN <18..28
FT /note="Lipoyl-binding 2"
FT /evidence="ECO:0000250|UniProtKB:P08461"
FT REGION 37..57
FT /note="E3- and/or E1-component binding domain"
FT /evidence="ECO:0000250|UniProtKB:P08461, ECO:0000255"
FT ACT_SITE 192
FT /evidence="ECO:0000250|UniProtKB:P08461, ECO:0000255"
FT ACT_SITE 196
FT /evidence="ECO:0000250|UniProtKB:P08461, ECO:0000255"
FT BINDING 187..198
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P08461"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10515"
FT MOD_RES 121
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMF4"
FT NON_CONS 17..18
FT /evidence="ECO:0000305"
FT NON_CONS 31..32
FT /evidence="ECO:0000305"
FT NON_CONS 40..41
FT /evidence="ECO:0000305"
FT NON_CONS 55..56
FT /evidence="ECO:0000305"
FT NON_CONS 63..64
FT /evidence="ECO:0000305"
FT NON_CONS 121..122
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 219 AA; 23117 MW; 11B4C4C826FE3B08 CRC64;
VPLPSLSPTM QAGTIARDVP LGAPLCIIVE KGRVFVSPLA KGIDLTQVKG TGPEGDIDSF
VPSKVPEANS SWMDTVIRQN HVVDVSVAVS TPAGLITPIV FNAHIKGLET IASDVVSLAS
KEGKLQPHEF QGGTFTISNL GMFGIKNFSA IINPPQACIL AIGASEDKLI PADNEKGFDV
ASVMSVTLSC DHRVVDGAVG AQWLAEFKKY LEKPITMLL
