ID A0A1A1YXP2_9MYCO Unreviewed; 392 AA.
AC A0A1A1YXP2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=A5724_14105 {ECO:0000313|EMBL:OBF36092.1};
OS Mycobacterium sp. ACS1612.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834117 {ECO:0000313|EMBL:OBF36092.1, ECO:0000313|Proteomes:UP000092025};
RN [1] {ECO:0000313|Proteomes:UP000092025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS1612 {ECO:0000313|Proteomes:UP000092025};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Kiyimba A., Mayanja H.,
RA Musoke P., Ssengooba W., Joloba M.;
RL Submitted (JUN-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}.
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:OBF36092.1}.
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DR EMBL; LZHZ01000026; OBF36092.1; -; Genomic_DNA.
DR RefSeq; WP_067800588.1; NZ_LZHZ01000026.1.
DR AlphaFoldDB; A0A1A1YXP2; -.
DR STRING; 1834117.A5724_14105; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000092025; 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; 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; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000092025};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 4..79
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 117..154
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 98..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 41655 MW; 44B54FEB2A17F70F CRC64;
MSAVKEFLVP DLGEGLEDAT ITGWSVAVGD EVELNQTLCT VETNKAEVEI PSPFAGRITE
LGGAEGDTLT VGSVLVRIAT SEAESTNGTA RKPVLVGYGA DDEMDSSRRR SVGERPRAKP
PVRKLAVELN VDLSAVAGTG PGGVITREDV LAAAGRSAPT PEMLAVRGVQ AEMAHRMTLS
RKQIPDAHAG VQVDCTSLLE MRDRFRDAVD DESPVTPFVL ILRLLTIALR RHPHLNATWL
ETTDGPQIHL HSAVHLGFGV AAPRGLLVPV ITDAHAKTTR EFVTVVAQLI RDARAGTLKP
SQLQGSTFTV SNFGALGLDD GVPVINYPEA AILGMGSLKP RPVVVDGDVV ARPTMSLTCA
FDHRIADGAQ VAAFLTELRD LIETPELALL DL
//
