ID A0A1Q4VQS4_9ACTN Unreviewed; 484 AA.
AC A0A1Q4VQS4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=A6A06_23715 {ECO:0000313|EMBL:OKI00174.1};
OS Streptomyces sp. CB02923.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718985 {ECO:0000313|EMBL:OKI00174.1, ECO:0000313|Proteomes:UP000185893};
RN [1] {ECO:0000313|EMBL:OKI00174.1, ECO:0000313|Proteomes:UP000185893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02923 {ECO:0000313|EMBL:OKI00174.1,
RC ECO:0000313|Proteomes:UP000185893};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI00174.1}.
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DR EMBL; LWKZ01000025; OKI00174.1; -; Genomic_DNA.
DR RefSeq; WP_073765525.1; NZ_LWKZ01000025.1.
DR AlphaFoldDB; A0A1Q4VQS4; -.
DR STRING; 1718985.A6A06_23715; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000185893; 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 Reference proteome {ECO:0000313|Proteomes:UP000185893};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 8..83
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 184..221
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 84..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 49782 MW; 15780E91D366EBE9 CRC64;
MTATEQRFRE FKMPDVGEGL TEAEILKWYV QPGDTVTDGQ VICEVETAKA AVELPSPYEG
VVHAVHFEEG ATVDVGTSII AVDTDPGAGP AGAPAAAEAA PAAAEEDAEP QGRQAVLVGY
GAAPSSTKRR ARKPQAGVPA QEPAAAAIQA ELNGHAAAPA PAPVAPAAPA PAVPAAVPAA
GRPLAKPPVR KLAKDLGIDL AAVTPTGPDG VITREDVHAA AAPAPAAEAP AAVPQPAADT
ATATGGSEAV RARETRIPIK GVRKATAQAM VNSAFTAPHV TEFVTVDVTR TMKLVQELKQ
DPDMAGLRVN PLLLVARALL VAIKRNPEVN AAWDEDNQEI IRKDYVNLGI AAATPRGLIV
PNIKDAEAKT LPQLATALGE LIATAREGKT APGDMAGGTV TITNVGVFGV DTGTPILNPG
ESAILAFGAV KLQPWVHKGK VKPRQVTTLA LSFDHRLVDG ELGSKVLADT AAILEQPKRL
ITWA
//
