ID A0A1B1MD57_STRLN Unreviewed; 477 AA.
AC A0A1B1MD57;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=GJU35_22055 {ECO:0000313|EMBL:QMV08070.1}, SLCG_4271
GN {ECO:0000313|EMBL:AXG55426.1}, SLINC_4332
GN {ECO:0000313|EMBL:ANS66556.1};
OS Streptomyces lincolnensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS66556.1, ECO:0000313|Proteomes:UP000092598};
RN [1] {ECO:0000313|EMBL:ANS66556.1, ECO:0000313|Proteomes:UP000092598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS66556.1,
RC ECO:0000313|Proteomes:UP000092598};
RA Meng S.C.;
RT "Enhancement of antibiotic productionsby engineered nitrateutilization in
RT actinobacteria.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AXG55426.1, ECO:0000313|Proteomes:UP000253884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC-G {ECO:0000313|EMBL:AXG55426.1,
RC ECO:0000313|Proteomes:UP000253884};
RX PubMed=29574602; DOI=10.1007/s10295-018-2029-1;
RA Xu Y., Tan G., Ke M., Li J., Tang Y., Meng S., Niu J., Wang Y., Liu R.,
RA Wu H., Bai L., Zhang L., Zhang B.;
RT "Enhanced lincomycin production by co-overexpression of metK1 and metK2 in
RT Streptomyces lincolnensis.";
RL J. Ind. Microbiol. Biotechnol. 45:345-355(2018).
RN [3] {ECO:0000313|EMBL:QMV08070.1, ECO:0000313|Proteomes:UP000515335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B48 {ECO:0000313|EMBL:QMV08070.1,
RC ECO:0000313|Proteomes:UP000515335};
RX PubMed=32322696;
RA Wang R., Kong F., Wu H., Hou B., Kang Y., Cao Y., Duan S., Ye J., Zhang H.;
RT "Complete genome sequence of high-yield strain S. lincolnensis B48 and
RT identification of crucial mutations contributing to lincomycin
RT overproduction.";
RL Synth Syst Biotechnol 5:37-48(2020).
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}.
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DR EMBL; CP016438; ANS66556.1; -; Genomic_DNA.
DR EMBL; CP022744; AXG55426.1; -; Genomic_DNA.
DR EMBL; CP046024; QMV08070.1; -; Genomic_DNA.
DR RefSeq; WP_067436305.1; NZ_CP046024.1.
DR AlphaFoldDB; A0A1B1MD57; -.
DR STRING; 1915.SLINC_4332; -.
DR KEGG; sls:SLINC_4332; -.
DR PATRIC; fig|1915.4.peg.4783; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000092598; Chromosome.
DR Proteomes; UP000253884; Chromosome.
DR Proteomes; UP000515335; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000092598};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 9..84
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 177..214
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 111..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 49476 MW; D6CA4DC7DB6A73DA CRC64;
MTTMTEASVR EFKMPDVGEG LTEAEILKWY VQPGDTVTDG QVVCEVETAK AAVELPIPYD
GVVRELRFGE GTTVDVGTAI ISVDVAGGGA AAAQAPEASA SAVAAAPAVS AEKKPEPSKP
AAGSGRQPVL VGYGVATSST KRRPRKGPEI PAQEASKAIQ SELNGHGAAA AAKPRPLAKP
PVRKLAKDLG VDLATVIPSG PDGIITREDV HAAVTPPQQA PEPVTAPPVT PVAAPAAPAA
SYDAARETRI PVRGVRKATA AAMVGSAFTA PHVTEFVTVD VTRTMKLVEE LKQDKEFQGL
RVNPLLLIAK ALLVAIRRNP DVNASWDEAA QEIVVKHYVN LGIAAATPRG LIVPNIKDAD
AKTLPQLAEG LAELVATARE GKTSPAAMQG GTVTITNVGV FGVDTGTPIL PPGESAILAV
GAIKLQPWVH KGKVKPRQVT TLALSFDHRL IDGELGSKVL ADVAAVLEQP KRLITWA
//
