ID I0L6S3_9ACTN Unreviewed; 402 AA.
AC I0L6S3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=MILUP08_44395 {ECO:0000313|EMBL:CCH19520.1};
OS Micromonospora lupini str. Lupac 08.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH19520.1, ECO:0000313|Proteomes:UP000003448};
RN [1] {ECO:0000313|Proteomes:UP000003448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448};
RX PubMed=22815450; DOI=10.1128/jb.00628-12;
RA Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., Vallenet D.,
RA Carro L., Coll P., Trujillo M.E.;
RT "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root
RT Nodules of Lupinus angustifolius.";
RL J. Bacteriol. 194:4135-4135(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCH19520.1}.
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DR EMBL; CAIE01000035; CCH19520.1; -; Genomic_DNA.
DR AlphaFoldDB; I0L6S3; -.
DR STRING; 1150864.MILUP08_44395; -.
DR eggNOG; COG0508; Bacteria.
DR Proteomes; UP000003448; 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 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 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 SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:CCH19520.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000003448};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:CCH19520.1}.
FT DOMAIN 16..69
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|Pfam:PF00364"
FT DOMAIN 180..399
FT /note="2-oxoacid dehydrogenase acyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00198"
SQ SEQUENCE 402 AA; 42066 MW; CC6E37880DBD12E9 CRC64;
MVTDLVVPKL NNNDTSYVLL DWLAEDGEQV RAGEPIAEVE TSKAAEELLS DGDGVLHRLV
EVNRECAPGD VIGHVFDSEE ARQRFLAAAV APPVVPLPDV SPGGPVLTDS ARELAAAHGL
GDDELRGLGR SVVRRTDVER LLADRSAAPA ATTEPVVVAA AAALAAGDGP EPDDPRPVHA
LSRAQRAVAA VVTESHREVP AALAVIKVRA DAALTVARDL TRATRTLVGL PELLVKAIGG
LREDHPLLFA SPGDGSSVRL AEAAHVGVTI DVGTGLFIPV VRDVEELTCA EIAETLMHFR
SRAGGEGFRA GELAGGTIVV SLHTDPDVVL AGPIVFPGQT CVVAIGGTQD ELALDTDGRV
VTRRFVNLSA VYDHRVVNGR EAVAFLQAVK AALESPDRLA EE
//
