ID A0A0N0A672_9ACTN Unreviewed; 264 AA.
AC A0A0N0A672;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Dihydrolipoamide acetyltransferase {ECO:0000313|EMBL:KOV91446.1};
DE Flags: Fragment;
GN ORFNames=ADL04_33365 {ECO:0000313|EMBL:KOV91446.1};
OS Streptomyces sp. NRRL B-3648.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519493 {ECO:0000313|EMBL:KOV91446.1, ECO:0000313|Proteomes:UP000037702};
RN [1] {ECO:0000313|EMBL:KOV91446.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-3648 {ECO:0000313|EMBL:KOV91446.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
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:KOV91446.1}.
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DR EMBL; LGDZ01000228; KOV91446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0A672; -.
DR PATRIC; fig|1519493.3.peg.7117; -.
DR Proteomes; UP000037702; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43416:SF8; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
DR SUPFAM; SSF51230; Single hybrid motif; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
PE 3: Inferred from homology;
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Reference proteome {ECO:0000313|Proteomes:UP000037702};
KW Transferase {ECO:0000313|EMBL:KOV91446.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 139..214
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 79..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..264
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 264
FT /evidence="ECO:0000313|EMBL:KOV91446.1"
SQ SEQUENCE 264 AA; 25315 MW; 953BBC762FC39F9A CRC64;
MAVSVTLPAL GESVTEGTVT RWLKAEGERV EADEPLLEVS TDKVDTEIPA PASGVLASIK
VAEDETVEVG AELALIDDGT GAPAAAPAPA AEAAPAAEPA PAPAAEPEPA PQAAPSTEQA
APAPAPTAEA ASGGGSAEGT DVVLPALGES VTEGTVTRWL KSVGDSVEAD EPLLEVSTDK
VDTEIPAPTS GVLLEITVGE DETAEVGAKL AVIGAPGAAP AAAPAPAAPA PAAAPAPAPE
PAPAPAPEPA PAPAPAPAPA PAPA
//