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Database: UniProt
Entry: A0A370H1Y3_9NOCA
LinkDB: A0A370H1Y3_9NOCA
Original site: A0A370H1Y3_9NOCA 
ID   A0A370H1Y3_9NOCA        Unreviewed;       593 AA.
AC   A0A370H1Y3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=DFR68_106463 {ECO:0000313|EMBL:RDI50025.1};
OS   Nocardia mexicana.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=279262 {ECO:0000313|EMBL:RDI50025.1, ECO:0000313|Proteomes:UP000255355};
RN   [1] {ECO:0000313|EMBL:RDI50025.1, ECO:0000313|Proteomes:UP000255355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44952 {ECO:0000313|EMBL:RDI50025.1,
RC   ECO:0000313|Proteomes:UP000255355};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUL-2018) 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:RDI50025.1}.
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DR   EMBL; QQAZ01000006; RDI50025.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A370H1Y3; -.
DR   STRING; 1210089.GCA_001613165_04080; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000255355; 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; 2.
DR   Gene3D; 2.40.50.100; -; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR014276; 2-oxoglutarate_DH_E2.
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   NCBIfam; TIGR02927; SucB_Actino; 1.
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; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
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; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000255355};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          131..206
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          281..318
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          83..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..123
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..260
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   593 AA;  59553 MW;  2A744295305692F9 CRC64;
     MAFSVQMPAL GESVTEGTVT RWLKQEGDTV EVDEPLLEVS TDKVDTEIPS PAAGVLTKIV
     AQEDDVVEVG GELGVIGEAG EAAASAPAPA PEAAAPAPAP AEAPAPEPAQ QPAAAPAPEP
     AAAPAPAAAS GTPVQMPELG ESVTEGTVTR WLKQVGDQIE VDEPLLEVST DKVDTEIPSP
     VAGTLLEISA NEDDVVAVGG QLGVIGSGSP AAAPAPAPAP APAPEPAPAP AAAAPAPPPA
     PAPAPAPAPA PAPAAPAPAA SAPAPAASAP ATSSGNGEAP YVTPLVRKLA AENNVDLSTV
     KGSGVGGRIR KQDVLAAAES TQAPAAAPAA APAAAPKAPA PSAAPAGVRP QLQALRGTVQ
     KASRIRQITA AKTRESLQTT AQLTQTHEVD VTKIAALRGK TKDAFKEREG VNLTFLPFFA
     KAAVEALGVH PNVNASYNEE TKEITYHSAV HLGIAVDTDQ GLLSPVIHNA SDLSLAGLAR
     AIADIAGRAR TGGLKPDELA GGTFTITNIG SQGALFDTPI LVPPQSAMLG TGAIVKRPMV
     IADNGNEFIG IRSVCFLPLT YDHRLIDGAD AGRFLTTIKH RLEEAAFEAD LGL
//
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