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Database: UniProt
Entry: A0A0N0A672_9ACTN
LinkDB: A0A0N0A672_9ACTN
Original site: A0A0N0A672_9ACTN 
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
//
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