ID   H0QM49_ARTGO            Unreviewed;       202 AA.
AC   H0QM49;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Dihydrolipoamide acyltransferase {ECO:0000313|EMBL:GAB13900.1};
GN   ORFNames=ARGLB_051_00810 {ECO:0000313|EMBL:GAB13900.1};
OS   Arthrobacter globiformis NBRC 12137.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1077972 {ECO:0000313|EMBL:GAB13900.1, ECO:0000313|Proteomes:UP000003828};
RN   [1] {ECO:0000313|EMBL:GAB13900.1, ECO:0000313|Proteomes:UP000003828}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12137 {ECO:0000313|EMBL:GAB13900.1,
RC   ECO:0000313|Proteomes:UP000003828};
RA   Miyazawa S., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Arthrobacter globiformis NBRC 12137.";
RL   Submitted (DEC-2011) 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:GAB13900.1}.
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DR   EMBL; BAEG01000051; GAB13900.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0QM49; -.
DR   STRING; 1077972.ARGLB_051_00810; -.
DR   eggNOG; COG0508; Bacteria.
DR   Proteomes; UP000003828; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase 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; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:GAB13900.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003828};
KW   Transferase {ECO:0000313|EMBL:GAB13900.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          130..202
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          73..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   202 AA;  20610 MW;  EDB128B04DE86784 CRC64;
     MSESVNLPAL GESVTEGTVT RWLKQVGDRV EVDEPLLEVS TDKVDTEIPS PIAGVIEEIL
     VAEDETAEVG APLVRIGDGS GGGAAEAPAA APAEEAPAAP AEESPAAPAE EAPAQEAPAA
     EAAPASSGEG HEVTLPALGE SVTEGTVTRW LKAVGDSVEV DEPLLEVSTD KVDTEIPSPW
     PAPCRKSAST RTRPPRLALS SP
//