ID E2PWQ1_STRCL Unreviewed; 507 AA.
AC E2PWQ1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=bkdC {ECO:0000313|EMBL:EFG08050.1};
GN ORFNames=SCLAV_2979 {ECO:0000313|EMBL:EFG08050.1};
OS Streptomyces clavuligerus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1901 {ECO:0000313|EMBL:EFG08050.1, ECO:0000313|Proteomes:UP000002357};
RN [1] {ECO:0000313|EMBL:EFG08050.1, ECO:0000313|Proteomes:UP000002357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 /
RC NRRL 3585 / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357};
RX PubMed=20624727; DOI=10.1093/gbe/evq013;
RA Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA Breitling R., Takano E.;
RT "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT evolutionary reservoir of secondary metabolic pathways.";
RL Genome Biol. Evol. 2:212-224(2010).
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; CM000913; EFG08050.1; -; Genomic_DNA.
DR RefSeq; WP_003961149.1; NZ_WMCC01000134.1.
DR AlphaFoldDB; E2PWQ1; -.
DR STRING; 1901.BB341_13680; -.
DR GeneID; 61470911; -.
DR KEGG; sclf:BB341_13680; -.
DR eggNOG; COG0508; Bacteria.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000002357; 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; 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 ECO:0000313|EMBL:EFG08050.1}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000002357};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EFG08050.1}.
FT DOMAIN 4..79
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 191..228
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 83..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 51335 MW; 808E2E5217B67A31 CRC64;
MAQVLEFRLP DLGEGLTEAE IVRWLVSVGD VVAVDQPVVE VETAKAMVEV PCPYGGVVTA
RFGEEGTELP VGAPLLTVAV GADADRRPGT DGDGQQGAHG GQGGQGGQGG QGGQGGAAAS
GPVAGAGPSG AVRGGAAESS GNVLVGYGTG APSARRRRLR PDPRTATGGS RAVAPVSDLD
EDADQSGPLP VISPLVRRLA RSYGLDLRQL SGSGPDGLIL RADVEYAMRA AGTALPGSAA
AAAGPATASP SAAASPSGAV ASSVSAPSSA VPSAPAEAAV ERIPLRGVRG AMADKLTRSR
SEIPDATCWV DADATELLAA RTAMNAAGGP KISIIALFAR ICAAALARHP ELNATVDTAA
REIVRLSAVH IGFAAQTERG LVVPVVKDAH RRSAESLTAE FARLTEAARE GRLSPAELTG
GTFTLNNYGV FGVDGSTPII NHPEAAMLGV GRIVAKPWVH RGELAVRQVV QLSLTFDHRV
CDGGTAGGFL RYVADCVEQP AVLLRTL
//
