ID   ODP2_ACHLA              Reviewed;         544 AA.
AC   P35489;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=E2;
GN   Name=pdhC;
OS   Acholeplasma laidlawii.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Acholeplasma.
OX   NCBI_TaxID=2148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1735725; DOI=10.1128/jb.174.4.1388-1396.1992;
RA   Wallbrandt P., Tegman V., Jonsson B.-H., Wieslander A.;
RT   "Identification and analysis of the genes coding for the putative pyruvate
RT   dehydrogenase enzyme complex in Acholeplasma laidlawii.";
RL   J. Bacteriol. 174:1388-1396(1992).
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).
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:0000305};
CC       Note=Binds 2 lipoyl cofactors covalently. {ECO:0000305};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; M81753; AAA21909.1; -; Genomic_DNA.
DR   PIR; C42653; C42653.
DR   AlphaFoldDB; P35489; -.
DR   SMR; P35489; -.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Direct protein sequencing; Glycolysis; Lipoyl; Repeat;
KW   Transferase.
FT   CHAIN           1..544
FT                   /note="Dihydrolipoyllysine-residue acetyltransferase
FT                   component of pyruvate dehydrogenase complex"
FT                   /id="PRO_0000162270"
FT   DOMAIN          1..76
FT                   /note="Lipoyl-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          113..188
FT                   /note="Lipoyl-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          242..279
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT   ACT_SITE        516
FT                   /evidence="ECO:0000255"
FT   MOD_RES         42
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
FT   MOD_RES         154
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
SQ   SEQUENCE   544 AA;  57261 MW;  81E92D869CFD5424 CRC64;
     MYEFKFADIG EGIHEGTVLQ WNFKVGDKVK EGETLVIVET DKVNAELPSP VDGTIVSLGA
     KEGEEIHVGQ IIVTIDDGTG TPAAAPAPAQ VSAPTPAPAA APQVAAPAAS GDIYDFKFAD
     IGEGIHEGTI LQWNFKVGDK VKEGETLVVV ETDKVNAELP SPVDGTILKL GKAEGEVIHV
     GETVVLIGQN GATLEQAQAP KAEAPVSEPK KGAGVVGEIE VSDDIIGGSE EVHVVATTGK
     VLASPVARKL ASDLGVDIAT IKGSGEQGRV MKDDVQNSKA PAEAQAPVQQ TQAPAQAAAS
     VAPSFAAAGK PQGDVEVVKI TRLRKAVSNA MTRSKSIIPE TVLMDEINVD ALVNFRNEAK
     GLAESKGIKL TYMAFIAKAV LIALKEFPMF NASFNHDTDE VYIKKFINLG MAVDTPDGLI
     VPNIKNADRL SVFELASQVR SLADDTIARK ISMDQQTGGT FTITNFGSAG IAFGTPVINY
     PELAILGIGK IDRKPWVVGN EIKIAHTLPL SLAVDHRIID GADGGRFLMR VKELLTNPTL
     LLLS