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Database: UniProt
Entry: A0A0D3CRS4_BRAOL
LinkDB: A0A0D3CRS4_BRAOL
Original site: A0A0D3CRS4_BRAOL 
ID   A0A0D3CRS4_BRAOL        Unreviewed;       456 AA.
AC   A0A0D3CRS4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   08-NOV-2023, entry version 39.
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=106298256 {ECO:0000313|EnsemblPlants:Bo6g044130.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo6g044130.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo6g044130.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo6g044130.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={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   RefSeq; XP_013589808.1; XM_013734354.1.
DR   AlphaFoldDB; A0A0D3CRS4; -.
DR   STRING; 109376.A0A0D3CRS4; -.
DR   EnsemblPlants; Bo6g044130.1; Bo6g044130.1; Bo6g044130.
DR   GeneID; 106298256; -.
DR   Gramene; Bo6g044130.1; Bo6g044130.1; Bo6g044130.
DR   KEGG; boe:106298256; -.
DR   eggNOG; KOG0557; Eukaryota.
DR   HOGENOM; CLU_016733_10_2_1; -.
DR   OMA; HSRVNKP; -.
DR   OrthoDB; 1399at2759; -.
DR   Proteomes; UP000032141; Chromosome C6.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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; IPR045257; E2/Pdx1.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR23151:SF75; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT 5 OF PYRUVATE DEHYDROGENASE COMPLEX, CHLOROPLASTIC; 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:UP000032141};
KW   Transferase {ECO:0000256|RuleBase:RU003423};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          39..114
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          178..215
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          122..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   456 AA;  47843 MW;  8F474186ABD14095 CRC64;
     MSRLLNTSFL PCSTCRTRSS SAPHSRVNKP RIVSVRAKIR EIFMPALSST MTEGKIVSWV
     KSEGDKLSKG ESVVVVESDK ADMDVETFYD GYLAAIMVEE GGVAPVGSAI ALLAETEEEI
     ADARAKASGG GGGTSPSPPV SQAPPVVEEK VSASVPPPKV VSSASAVHPA SEGGKRVVAS
     PYAKKLAKEL KVELAALVGS GPMGRIVAKD VEAAVAAAPP VQKEAMAPAV AVELGSVVPF
     TTMQGAVSRN MVESLSVPTF RVGYTINTDA LDALYKKIKS KGVTMTALLA KATALALAKH
     PVVNSSCRDG NSFVYNSSIN IAVAVAIDGG LITPVLQNAD KVDIYSLSRK WKELVDKARA
     KQLQPQEYNT GTFTLSNLGM FGVDRFDAIL PPGTGAIMAV GASQPTVVAT KDGRIGMKNQ
     MQVNVTADHR VIYGADLAQF LQTLASIIED PKDLTF
//
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