ID A0A0C5B6W8_9MOLU Unreviewed; 428 AA.
AC A0A0C5B6W8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:AJM71922.1};
GN ORFNames=MYE_02215 {ECO:0000313|EMBL:AJM71922.1};
OS Mycoplasma yeatsii GM274B.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=743967 {ECO:0000313|EMBL:AJM71922.1, ECO:0000313|Proteomes:UP000032020};
RN [1] {ECO:0000313|EMBL:AJM71922.1, ECO:0000313|Proteomes:UP000032020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM274B {ECO:0000313|EMBL:AJM71922.1,
RC ECO:0000313|Proteomes:UP000032020};
RX PubMed=25908137; DOI=10.1128/genomeA.00328-15;
RA Calcutt M.J., Kent B.N., Foecking M.F.;
RT "Complete genome sequence of Mycoplasma yeatsii strain GM274B (ATCC
RT 43094).";
RL Genome Announc. 3:0-0(2015).
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; CP007520; AJM71922.1; -; Genomic_DNA.
DR RefSeq; WP_042733354.1; NZ_CP007520.1.
DR AlphaFoldDB; A0A0C5B6W8; -.
DR STRING; 743967.MYE_02215; -.
DR KEGG; myt:MYE_02215; -.
DR PATRIC; fig|743967.3.peg.440; -.
DR HOGENOM; CLU_016733_10_0_14; -.
DR Proteomes; UP000032020; 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:AJM71922.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:AJM71922.1};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AJM71922.1}.
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 134..171
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 83..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 45762 MW; AC386D2E47FAC2FF CRC64;
MYQVKFADIG EGLTEGTVAE VLVKVGDVVK AGQPLYFVET DKVNSEIPAP IDGKIAVINI
KAGQEIKVGE VVMEIEDGAS AEACPKDGAC SSSKEAKSEP VEENASVIGA TPVSNELLVR
NIPKTTSLAQ QVIKATPLAR KVAADLNVDL SSIQGTGPNG RILVADVKGS QPSVQVQPAS
VQEQPAPIKR LLDIDAPLSW DTINMNGIRK ATVKAMVKSH TEIAAFSGMK NVDITETYKL
RSDLKDSAAS QGVKLTYLAF IIKACAKALR DMPNINARGD FANNKIQYMH NINIGIAVDT
PQGLMVPVIK GADLLSVFEI ANKISELANK AKEGKLSMKE MSEATFTVSN FGSVGLDYAT
PIINSPESAI LGVGTMTQTP MYINGEIQPR FIMPFSMTCD HRIIDGADAG RFLVKVQEYL
AKPIALFV
//
