ID   ODP2_MYCCT              Reviewed;         438 AA.
AC   Q49110; Q2SSP9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 126.
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; Synonyms=odp2; OrderedLocusNames=MCAP_0227;
OS   Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS   / NCTC 10154).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=340047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8844861; DOI=10.1002/pro.5560050825;
RA   Zhu P.P., Peterkofsky A.;
RT   "Sequence and organization of genes encoding enzymes involved in pyruvate
RT   metabolism in Mycoplasma capricolum.";
RL   Protein Sci. 5:1719-1736(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA   Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA   Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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) (By similarity). {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   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC       Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
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; U62057; AAC44344.1; -; Genomic_DNA.
DR   EMBL; CP000123; ABC01559.1; -; Genomic_DNA.
DR   RefSeq; WP_011387115.1; NC_007633.1.
DR   AlphaFoldDB; Q49110; -.
DR   SMR; Q49110; -.
DR   EnsemblBacteria; ABC01559; ABC01559; MCAP_0227.
DR   GeneID; 23778820; -.
DR   KEGG; mcp:MCAP_0227; -.
DR   HOGENOM; CLU_016733_10_0_14; -.
DR   OMA; HPCIMAP; -.
DR   OrthoDB; 1626282at2; -.
DR   PhylomeDB; Q49110; -.
DR   Proteomes; UP000001928; Chromosome.
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; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Glycolysis; Lipoyl; Transferase.
FT   CHAIN           1..438
FT                   /note="Dihydrolipoyllysine-residue acetyltransferase
FT                   component of pyruvate dehydrogenase complex"
FT                   /id="PRO_0000162280"
FT   DOMAIN          1..76
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          132..169
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT   REGION          172..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        411
FT                   /evidence="ECO:0000255"
FT   MOD_RES         42
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
SQ   SEQUENCE   438 AA;  46927 MW;  4BF83B697480B4AB CRC64;
     MFKVKFADIG EGLTEGTVAE VLVKVGDVVK EGQSLYFVET DKVNSEIPAP VAGKIAVINI
     KAGQEIKVGD VVMEIEDGSD TSATSEPKAE TKSEAKVEVV EENASVVGAT PVSNDVIVRK
     QTTTVNKSST IKATPLARKV AADLNIDLSL VTPTGPNQRI LVADIKNHQA SSTQLASQPI
     SQPAPTPSPS AHQTIAPTIK VVEPSAPLSW DEVPMNGVRK ATVKAMTKSH TEIAAFTGMK
     NTDITETHKM RTELKDHAAA SGIKLTYLAF IIKAVAKSLR DMPNINVRGD FANNKIQFMH
     NINIGIAVDT PNGLMVPVIK GADHLSVFEI AIKISELANK AKDGKLTRAE MTEATFTVSN
     FGSVGLDYAT PIINSPESAI LGVGTMSQTP LYINGELQKR FIMPLSMTCD HRIIDGADAG
     RFLIKVQDYL SKPVLLFM