ID A0A0Q9TGU9_9ACTN Unreviewed; 513 AA.
AC A0A0Q9TGU9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=ASG94_11410 {ECO:0000313|EMBL:KRF34771.1};
OS Nocardioides sp. Soil805.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736416 {ECO:0000313|EMBL:KRF34771.1, ECO:0000313|Proteomes:UP000051356};
RN [1] {ECO:0000313|EMBL:KRF34771.1, ECO:0000313|Proteomes:UP000051356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil805 {ECO:0000313|EMBL:KRF34771.1,
RC ECO:0000313|Proteomes:UP000051356};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF34771.1, ECO:0000313|Proteomes:UP000051356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil805 {ECO:0000313|EMBL:KRF34771.1,
RC ECO:0000313|Proteomes:UP000051356};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRF34771.1}.
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DR EMBL; LMSU01000002; KRF34771.1; -; Genomic_DNA.
DR RefSeq; WP_056926594.1; NZ_LMSU01000002.1.
DR AlphaFoldDB; A0A0Q9TGU9; -.
DR STRING; 1736416.ASG94_11410; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000051356; 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; IPR003016; 2-oxoA_DH_lipoyl-BS.
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; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 219..256
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 79..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 53116 MW; 6629B252802BE5B1 CRC64;
MSEFKLPDVG EGLTEAEIVS WKVKAGDSVE INDIIVEIET AKSIVELPSP YAGTVLALMV
DEGQMVDVGT PIISIGSASD AAPAAPVTPA STAAQTESDP YLGMAQKAAA VDLSDMDLSN
PAASGGGEGE SLVGRNKAER GPQRRARKGS ATPSTAAGAQ TQMQLQGAFA PGGAQTDEVA
AVDEPAVPAT SAAPARPSDP APALVPPSVQ TPRGDVRALA KPPVRKLAKD LGVDLTLLTG
AGPGGVITRA DVEAAASGSG TDNGWAPAAE PATTRRTGEG PRETREPIKG VRKMMAQAMS
QSAFTSPHVT EWITVDVTAT MQLVERLKAR RELREVRVSP LLVLSRAVLL AIKRTPEINS
YWDDAAQEVV HKHYVNLGIA AATPRGLVVP NVKDADSMSM VELAGALGEL TATARDGKTQ
PAEMAGGTFT ITNVGVFGVD AGTPIINPGE SAILCFGAIN KRPWVSEEGE IVVRDVTTLA
LSFDHRHIDG EKGSRFLADV AGILADPGSA LLF
//
