ID A0A061FRR1_THECC Unreviewed; 471 AA.
AC A0A061FRR1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=TCM_036333 {ECO:0000313|EMBL:EOY17179.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY17179.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY17179.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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 EMBL; CM001886; EOY17179.1; -; Genomic_DNA.
DR RefSeq; XP_007019954.1; XM_007019892.2.
DR AlphaFoldDB; A0A061FRR1; -.
DR SMR; A0A061FRR1; -.
DR STRING; 3641.A0A061FRR1; -.
DR EnsemblPlants; EOY17179; EOY17179; TCM_036333.
DR EnsemblPlants; Tc08v2_t014600.1; Tc08v2_p014600.1; Tc08v2_g014600.
DR GeneID; 18592930; -.
DR Gramene; EOY17179; EOY17179; TCM_036333.
DR Gramene; Tc08v2_t014600.1; Tc08v2_p014600.1; Tc08v2_g014600.
DR KEGG; tcc:18592930; -.
DR eggNOG; KOG0557; Eukaryota.
DR HOGENOM; CLU_016733_10_2_1; -.
DR InParanoid; A0A061FRR1; -.
DR OMA; MDIEVKM; -.
DR OrthoDB; 1399at2759; -.
DR Proteomes; UP000026915; Chromosome 8.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IBA:GO_Central.
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 ECO:0000313|EMBL:EOY17179.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Transferase {ECO:0000256|RuleBase:RU003423};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 37..112
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 183..220
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 121..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 49345 MW; 0A6267378DC87553 CRC64;
MAHILQTSFL PFTSSLRRTP VSGPKGKPQA LQVKAKIREI FMPALSSTMT EGKIVSWTKS
EGEKLSKGES VVVVESDKAD MDVESFHDGF LAAIMVEEGG VAPVGSAIAL LAETEDEIAE
AKAKSQSSSS SSAQVLEEKP QEKEEVAPAV PAAAPVAPAV WSPKAVAVGS AVHPASEGGK
RIVASPYAKK LAKELKVDLV ALVGTGPMGR IVAKDVEAAA AAGVVAASES APLPASPEKA
APVAPEIELG TVVPFTTMQG AVSRNMVESL SVPTFRVGYT ITTNALDALY KKIKSKGVTM
TALLAKATAL ALVQHPVVNS CCRDGNSFTF NSSINIAVAV AIDGGLITPV LQDADKVDIY
TLSRKWKELV DKARAKQLQP HEYNTGTFTL SNLGMFGVDR FDAILPPGTG AIMAVGASLP
TVVASKDGRI GMQNQMQVNV TADHRVIYGA DLASFLQTLA KIIEDPKDLT F
//
