ID Q6MTX8_MYCMS Unreviewed; 428 AA.
AC Q6MTX8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=pdhC {ECO:0000313|EMBL:CAE76908.1};
GN OrderedLocusNames=MSC_0267 {ECO:0000313|EMBL:CAE76908.1};
OS Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272632 {ECO:0000313|EMBL:CAE76908.1, ECO:0000313|Proteomes:UP000001016};
RN [1] {ECO:0000313|EMBL:CAE76908.1, ECO:0000313|Proteomes:UP000001016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1 {ECO:0000313|EMBL:CAE76908.1,
RC ECO:0000313|Proteomes:UP000001016};
RX PubMed=14762060; DOI=10.1101/gr.1673304;
RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA Johansson K.-E., Pettersson B., Uhlen M.;
RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL Genome Res. 14:221-227(2004).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR EMBL; BX293980; CAE76908.1; -; Genomic_DNA.
DR RefSeq; NP_975266.1; NC_005364.2.
DR AlphaFoldDB; Q6MTX8; -.
DR STRING; 272632.MSC_0267; -.
DR KEGG; mmy:MSC_0267; -.
DR PATRIC; fig|272632.4.peg.288; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_14; -.
DR Proteomes; UP000001016; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 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 PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:CAE76908.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000001016};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:CAE76908.1}.
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 132..169
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 428 AA; 45827 MW; 11D4F196F49C16B4 CRC64;
MFKVKFADIG EGLTEGIVAE VLVKVGDVVK EGQSLYFVET DKVNSEIPAP VAGKIAVINI
KAGQEIKVGD VVMEIDEGTG ASVASEPKAE AKSEAKVEVV EENASVVGAT PVSNDLIVRK
QASTVAKSST IKATPLARKV AADLNVDLSL VTPTGPNQRI LVADIKNYHS SSAQPVSQPA
PAPVVTPTIK VVEPSAPLSW DEVPMNGVRK ATVKAMTKSH TEIAAFTGMK NTDITETHKM
RTELKDHAAA SGIKLTYLAF IIKAVAKSLR DMPNINVRGD FANNKIQFMH NINIGIAVDT
PNGLMVPVIK GVDHLSVFEI AIKINELANK AKDGKLTRAE MTEATFTVSN FGSVELDYAT
PIINSPESAI LGVGAMSQTP LYINGELQKR FIMPLSMTCD HRIIDGADAG RFLIKVQDYL
SKPVLLFM
//
