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Database: UniProt
Entry: A0A0E0L6S8_ORYPU
LinkDB: A0A0E0L6S8_ORYPU
Original site: A0A0E0L6S8_ORYPU 
ID   A0A0E0L6S8_ORYPU        Unreviewed;       510 AA.
AC   A0A0E0L6S8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC06G00280.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC06G00280.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC06G00280.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-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   AlphaFoldDB; A0A0E0L6S8; -.
DR   STRING; 4537.A0A0E0L6S8; -.
DR   EnsemblPlants; OPUNC06G00280.1; OPUNC06G00280.1; OPUNC06G00280.
DR   Gramene; OPUNC06G00280.1; OPUNC06G00280.1; OPUNC06G00280.
DR   eggNOG; KOG0557; Eukaryota.
DR   HOGENOM; CLU_016733_10_2_1; -.
DR   OMA; ATIEWEA; -.
DR   Proteomes; UP000026962; Chromosome 6.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0050734; F:hydroxycinnamoyltransferase activity; IEA:UniProt.
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; 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:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE 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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          225..262
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          178..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..220
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   510 AA;  55793 MW;  0757A68FB3C9CF16 CRC64;
     MALLLRHSPK LRRVHAILGC ERGSVVRHFS SSTCSSIVKE DTVSSSNLHP EYAKKIGGSN
     FSHDRQSRKE LQNFKVSPQE ARRTSNFMRA SKHGMLISAN GVVPARCFSS GADLPPHQEI
     GMPSLSPTMT EGNIARWVKK EGDKVSPGEV LCEVETIIAV TVEEEEYIDK FKDYKAPSSA
     ESAAPAESKP QSEPTEPKEE KEQPKAPEPK ATKTEESFLS EDRTFSSPIA RKLAEDNNVP
     LSSIKGTGPD GRILKADIED YLASMAKGAK KETAAAPGLG YVDLPNTQIR KVTANRLLHS
     KQTIPHYYLT VDTRVDKLIK LRSELNPLQD NSGGKKISIN DLVIKAAALA LRKVPECNSS
     WMNDFIRQYH NVNINVAVQT EHGLFVPVIR DADKKGLATI ADEVKQLAQR ARDNSLKPED
     YEGGTFTVSN LGGPFGIKQF CAIVNPPQSA ILAIGSAEKR VIPGAEGQFE VGSFMSATLS
     CDHRVIDGAI GAEWMKAFKG YIENPTTMLL
//
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