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Database: UniProt
Entry: G7CJE4_MYCT3
LinkDB: G7CJE4_MYCT3
Original site: G7CJE4_MYCT3 
ID   G7CJE4_MYCT3            Unreviewed;       396 AA.
AC   G7CJE4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=KEK_17623 {ECO:0000313|EMBL:EHI12742.1};
OS   Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP
OS   105390 / JCM 6362 / NCTC 10409 / 316) (Mycobacterium thermoresistibile).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1078020 {ECO:0000313|EMBL:EHI12742.1, ECO:0000313|Proteomes:UP000004915};
RN   [1] {ECO:0000313|EMBL:EHI12742.1, ECO:0000313|Proteomes:UP000004915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 /
RC   316 {ECO:0000313|Proteomes:UP000004915};
RG   Tuberculosis Structural Genomics Consortium;
RA   Ioerger T.R.;
RL   Submitted (NOV-2011) 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:EHI12742.1}.
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DR   EMBL; AGVE01000046; EHI12742.1; -; Genomic_DNA.
DR   RefSeq; WP_003927006.1; NZ_AGVE01000046.1.
DR   AlphaFoldDB; G7CJE4; -.
DR   PATRIC; fig|1078020.3.peg.3476; -.
DR   eggNOG; COG0508; Bacteria.
DR   Proteomes; UP000004915; 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:UP000004915};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          5..80
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          116..154
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          95..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   396 AA;  41662 MW;  04C47D333EC2CF8D CRC64;
     MNGSIREFLL PDLGEGLEDA TITDWSVTVG DEVELNQPLC TVETNKAEVE IPSPYAGRIV
     ELGGAAGETL PVGAVLVRIE TSSAGADRDP VLVGYGADDA MDTSRRTPHR ATGRPRAKPP
     VRRLAADLGV DLTAVAPGSG PDGVITRQDV LAAAGADGAD APAAPADAAD VVEVGAVQAA
     MARRMTQSRR EIPDAHGRVE VDCRALLELC AQLGERTVTP FVLTLRLLGI ALQHHPNLNA
     TWRDTDDGPR IHRHRAVHLG IAVSAPRGLL VPVVADAHRM TLPQLGAAVE RLVDRARAGT
     LTPAELTGST FTVSNFGALG LDDGVPVINY PEAAILGMGM IKPRPVVIDD AVVARPTMTL
     TCAFDHRVAD GAQVAAFLDE LRGLIESPSR ALLFLR
//
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