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Database: UniProt
Entry: A0A2K8PJB8_STRLA
LinkDB: A0A2K8PJB8_STRLA
Original site: A0A2K8PJB8_STRLA 
ID   A0A2K8PJB8_STRLA        Unreviewed;       432 AA.
AC   A0A2K8PJB8;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
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:ATZ25725.1};
GN   ORFNames=SLAV_19505 {ECO:0000313|EMBL:ATZ25725.1}, SLLC_17605
GN   {ECO:0000313|EMBL:QUQ55553.1};
OS   Streptomyces lavendulae subsp. lavendulae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=58340 {ECO:0000313|EMBL:ATZ25725.1, ECO:0000313|Proteomes:UP000231791};
RN   [1] {ECO:0000313|EMBL:ATZ25725.1, ECO:0000313|Proteomes:UP000231791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 3239 {ECO:0000313|EMBL:ATZ25725.1,
RC   ECO:0000313|Proteomes:UP000231791};
RA   Busche T., Novakova R., Al'Dilaimi A., Homerova D., Feckova L.,
RA   Rezuchova B., Mingyar E., Csolleiova D., Bekeova C., Winkler A.,
RA   Sevcikova B., Kalinowski J., Kormanec J., Ruckert C.;
RT   "Complete genome sequence of Streptomyces lavendulae subsp. lavendulae CCM
RT   3239 (formerly 'Streptomyces aureofaciens CCM 3239'), the producer of the
RT   angucycline-type antibiotic auricin.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QUQ55553.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Del-LP {ECO:0000313|EMBL:QUQ55553.1};
RA   Novakova R., Ruckert C., Knirschova R., Feckova L., Busche T.,
RA   Csolleiova D., Homerova D., Rezuchova B., Javorova R., Sevcikova B.,
RA   Kalinowski J., Kormanec J.;
RT   "The linear plasmid pSA3239 is essential for the replication of the
RT   Streptomyces lavendulae subsp. lavendulae CCM 3239 chromosome.";
RL   Submitted (APR-2021) 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}.
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DR   EMBL; CP024985; ATZ25725.1; -; Genomic_DNA.
DR   EMBL; CP073778; QUQ55553.1; -; Genomic_DNA.
DR   RefSeq; WP_030225085.1; NZ_JOEW01000002.1.
DR   AlphaFoldDB; A0A2K8PJB8; -.
DR   GeneID; 82165873; -.
DR   KEGG; slx:SLAV_19505; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000231791; Chromosome.
DR   Proteomes; UP000676025; 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:ATZ25725.1}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231791};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ATZ25725.1}.
FT   DOMAIN          4..79
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          148..185
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          89..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   432 AA;  44929 MW;  1A86ADF287C76363 CRC64;
     MPQVLEFKLP DLGEGLTEAE IVRWLVAVGD VVEIDQPVVE VETAKAMVEV PCPYGGVVTA
     RFGEEGTELP VGAPLITVAV GSVTEPAQAA EAEAEGSGNV PRPLIGYGTD HSRPARRRRV
     RPVTAAVSAP PVVAVAAAAP APAGPVPVIS PLVRKLARDN GIDLRALRGS GPEGLILRAD
     VEAALRPAAP AAAPAPVAAA AAAQGERIPL KGLRGAVAEK LSRSRREIPE ATCWVDADAT
     ELMAARAAMN AVDGPKISVL ALLARICTAA LAKYPELNST VDLAANEIVR LPAVHLGFAA
     QTERGLMVPV VRDAQTRSPE SLSAEFARLT ELARAGKLAP ADLTGGTFTL NNYGVFGVDG
     STPIINHPEA AMLGVGRIIP KPWVYRGELA VRQVVQLSLT FDHRVCDGGA AGGFLRYVAD
     CVENPAVLLR GL
//
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