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Database: UniProt
Entry: A0A0D3BA23_BRAOL
LinkDB: A0A0D3BA23_BRAOL
Original site: A0A0D3BA23_BRAOL 
ID   A0A0D3BA23_BRAOL        Unreviewed;       484 AA.
AC   A0A0D3BA23;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=106336425 {ECO:0000313|EnsemblPlants:Bo3g060860.1};
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:Bo3g060860.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo3g060860.1, 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:Bo3g060860.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|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   RefSeq; XP_013630714.1; XM_013775260.1.
DR   AlphaFoldDB; A0A0D3BA23; -.
DR   STRING; 109376.A0A0D3BA23; -.
DR   EnsemblPlants; Bo3g060860.1; Bo3g060860.1; Bo3g060860.
DR   GeneID; 106336425; -.
DR   Gramene; Bo3g060860.1; Bo3g060860.1; Bo3g060860.
DR   KEGG; boe:106336425; -.
DR   eggNOG; KOG0558; Eukaryota.
DR   HOGENOM; CLU_016733_10_0_1; -.
DR   OMA; MPFCIKA; -.
DR   OrthoDB; 1399at2759; -.
DR   Proteomes; UP000032141; Chromosome C3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:RHEA.
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:UP000032141};
KW   Transferase {ECO:0000256|RuleBase:RU003423};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          77..154
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          188..225
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   484 AA;  52904 MW;  96C38FAED5CCED26 CRC64;
     MIARRIWRSH RFLRPFSSSS VCAPPLLAPY HSQSFASPKS RPFLVPSLSL MKWCEGGGGS
     RSWFSNEAMT LDSDAGGGFI DVPLAQTGEG IAECELLKWF VKEGDPVEEF QPLCEVQSDK
     ATIEITSRFK GKVALISHAP GDIIKVGETL VKLAVEDSHD ALLVSSDTPG NVEPICSQPK
     LDTLVGALST PAVRTLAKDI GIDINLVTGS GKDGRVLKED VLQFSGQKQN VTDSAPSDNP
     FIRGDSVSTS FEDQIVPLRG FNRAMVKTMT MATKVPHFHF VEEINCNALV KLKHFFKEHN
     TDSTVKHTFL PTLIKSLSMA LTKYPYVNGC FNEESLEIIL KGSHNIGVAM ATEHGLVVPN
     IKNVQSLSLL EITREMSRLQ HLATNNKLSP EDVTGGTITL SNIGAIGGKF GSPLLNLPEV
     AIIALGRIEK VPKFKEDGSV YPASTMMVNI AADHRVLDGA TVARFCCQWK EYIEKPELLM
     LQMR
//
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