ID   ODP2_MYCPN              Reviewed;         402 AA.
AC   P75392;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 117.
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; OrderedLocusNames=MPN_391; ORFNames=MP447;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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   -!- INTERACTION:
CC       P75392; P02751: FN1; Xeno; NbExp=2; IntAct=EBI-2259593, EBI-1220319;
CC       P75392; P02788: LTF; Xeno; NbExp=3; IntAct=EBI-2259593, EBI-1058602;
CC       P75392; P00747: PLG; Xeno; NbExp=5; IntAct=EBI-2259593, EBI-999394;
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; U00089; AAB96095.1; -; Genomic_DNA.
DR   PIR; S73773; S73773.
DR   RefSeq; NP_110079.1; NC_000912.1.
DR   RefSeq; WP_010874747.1; NC_000912.1.
DR   AlphaFoldDB; P75392; -.
DR   SMR; P75392; -.
DR   IntAct; P75392; 5.
DR   STRING; 272634.MPN_391; -.
DR   PRIDE; P75392; -.
DR   EnsemblBacteria; AAB96095; AAB96095; MPN_391.
DR   GeneID; 66608950; -.
DR   KEGG; mpn:MPN_391; -.
DR   PATRIC; fig|272634.6.peg.422; -.
DR   HOGENOM; CLU_016733_10_0_14; -.
DR   OMA; HPCIMAP; -.
DR   BioCyc; MetaCyc:MON-584; -.
DR   BioCyc; MPNE272634:G1GJ3-618-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0009986; C:cell surface; IDA:AgBase.
DR   GO; GO:0005829; C:cytosol; IDA:AgBase.
DR   GO; GO:0016020; C:membrane; IDA:AgBase.
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   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; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Glycolysis; Lipoyl; Reference proteome; Transferase.
FT   CHAIN           1..402
FT                   /note="Dihydrolipoyllysine-residue acetyltransferase
FT                   component of pyruvate dehydrogenase complex"
FT                   /id="PRO_0000162282"
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   REGION          82..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..107
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..164
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        374
FT                   /evidence="ECO:0000255"
FT   MOD_RES         43
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
SQ   SEQUENCE   402 AA;  42397 MW;  F09314A9E714A1D6 CRC64;
     MANEFKFTDV GEGLHEGKVT EILKKVGDTI KVDEALFVVE TDKVTTELPS PYAGVITAIT
     TNVGDVVHIG QVMAVIDDGA GAAAPAAPQP VSAPAPAPTP TFTPTPAPVT TEPVVEEAGA
     SVVGEIKVSN SVFPIFGVQP SAPQPTPAPV VQPTSAPTPT PAPASAAAPS GEETIAITTM
     RKAIAEAMVK SHENIPATIL TFYVNATKLK QYRESVNGLA LSKYNMKISF FAFFVKAIVN
     ALKKFPVFNG RYDKERNLIV LNKDVNVGIA VDTPDGLIVP NIKQAQTKSV VDIAKDIVDL
     ANRARSKQIK LPDLSKGTIS VTNFGSLGAA FGTPIIKHPE MCIVATGNME ERVVRAEGGV
     AVHTILPLTI AADHRWVDGA DVGRFGKEIA KQIEELIDLE VA