ID A0A1I1YUG8_9ACTN Unreviewed; 492 AA.
AC A0A1I1YUG8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=SAMN05216251_102183 {ECO:0000313|EMBL:SFE23119.1};
OS Actinacidiphila alni.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=380248 {ECO:0000313|EMBL:SFE23119.1, ECO:0000313|Proteomes:UP000199323};
RN [1] {ECO:0000313|EMBL:SFE23119.1, ECO:0000313|Proteomes:UP000199323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3510 {ECO:0000313|EMBL:SFE23119.1,
RC ECO:0000313|Proteomes:UP000199323};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FONG01000002; SFE23119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1YUG8; -.
DR STRING; 380248.SAMN05216251_102183; -.
DR Proteomes; UP000199323; Unassembled WGS sequence.
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 Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:SFE23119.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199323};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:SFE23119.1}.
FT DOMAIN 18..93
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 202..239
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 94..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 50395 MW; 71F2F5D8AC2F8593 CRC64;
MTTMTAPQAG PRGQAQRFRE FRMPDVGEGL TEAEILKWYV SVGDTVTDGQ VICEVETAKA
AVELPIPYDG VISEIRFDEG TTVDVGTPII VVDAGPAAGG DAPAEPPADP SAGAVAPAGD
EPAANGEPKR QAVLVGYGVA PSSTTRRPRK ATASSAPAAA PAVPAQGAEL NGHARTAAAA
VPGAAPASAP ATGTAPAGER PLAKPPVRKL AKDLGIDLAT VVPTGPGGVV TRDDIRAAAA
PPATLPAAEQ APADAVPAGA RETRIPIKGV RKATAQAMVT SAFTAPHVTE FVTLDITRSM
KLVQELKEDR AFAGLRVSPL LLVAKALLVA LKRHPEANAA WDEAAQEIVQ KAYVNLGIAA
ATPRGLIVPN IKDAHDKTLP ELAAALGELV STARDGKTSP AAMQGGTVTI TNVGVFGVDT
GTPILNPGES AILAFGAVKL QPWVHKGKVK PRQVTTLALS FDHRLIDGEL GSKVLADVAA
ILEQPKRLLT WA
//
