ID A0A176QH25_9MICO Unreviewed; 468 AA.
AC A0A176QH25;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AWH69_04555 {ECO:0000313|EMBL:OAB89029.1};
OS Janibacter melonis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=262209 {ECO:0000313|EMBL:OAB89029.1, ECO:0000313|Proteomes:UP000076976};
RN [1] {ECO:0000313|EMBL:OAB89029.1, ECO:0000313|Proteomes:UP000076976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD11-4 {ECO:0000313|EMBL:OAB89029.1,
RC ECO:0000313|Proteomes:UP000076976};
RA Nair G.R., Kaur G., Chander A.M., Mayilraj S.;
RT "Janibacter melonis strain CD11_4 genome sequencing and assembly.";
RL Submitted (JAN-2016) 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:OAB89029.1}.
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DR EMBL; LQZG01000001; OAB89029.1; -; Genomic_DNA.
DR RefSeq; WP_068272072.1; NZ_LQZG01000001.1.
DR AlphaFoldDB; A0A176QH25; -.
DR STRING; 262209.AWH69_04555; -.
DR Proteomes; UP000076976; 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:UP000076976};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 170..207
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 85..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 468 AA; 48541 MW; CC2E57BF0586DC3B CRC64;
MALQKFILPD PGEGLTEADL VTWRVAVGDV VKVNDMVVEV ETAKSLVELP IPFAGTVVEL
LAAEGDTVDV GAPIIVVDTG GEAAPAVAPS AGSATAEEPD EASGPNLVGY GAKAGSTRRR
ARRGEPAQAS LPTEQPVAYS PAPPVEATPQ PEPAPAAPAA PVTGERARAL AKPPVRKMAK
DLGVDLSAVT PSGPGGVVTR EDVQAAASGA STSASSGGLE GRPAQLDQQA GPAERRVPIK
GVRKVTAQAM VDSAFTAPHV TEFVTVDVTA TMDLVDRLKK DRAFRDVKVT PLLVVAKALC
LAIRRNPDVN ASWDEAAQEI VYRRDVNLGI AAATPRGLVV PNIKGADSMP MRELADAMAQ
LVATAREGRT QPADFAGGTV TITNVGVFGV DTGTPILNPG EAAILAFGAV RRMPWVVERD
GVESIEPRWV TQLALSFDHR MVDGELGSKV LADVAALLHD PGQALVWA
//
