ID A0A1U7WQG3_NICSY Unreviewed; 466 AA.
AC A0A1U7WQG3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=LOC104229812 {ECO:0000313|RefSeq:XP_009780823.1};
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009780823.1};
RN [1] {ECO:0000313|Proteomes:UP000189701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA Peitsch M.C., Ivanov N.V.;
RT "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT tomentosiformis.";
RL Genome Biol. 14:R60.1-R60.17(2013).
RN [2] {ECO:0000313|RefSeq:XP_009780823.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_009780823.1};
RG RefSeq;
RL Submitted (NOV-2023) 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_009780823.1; XM_009782521.1.
DR STRING; 4096.A0A1U7WQG3; -.
DR GeneID; 104229812; -.
DR KEGG; nsy:104229812; -.
DR eggNOG; KOG0557; Eukaryota.
DR OrthoDB; 1399at2759; -.
DR Proteomes; UP000189701; Unplaced.
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:SF83; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT 4 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 Pyruvate {ECO:0000313|RefSeq:XP_009780823.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189701};
KW Transferase {ECO:0000256|RuleBase:RU003423};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 48..126
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 171..208
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 135..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 48708 MW; 91D240893CA84B47 CRC64;
MASLLQSKSP ALSFSSTISS PSSLRSSAAA TAAAFPRQYK LPVVQSKIRE IFMPALSSTM
TEGKIVSWTK SEGDVLSKGE SVVVVESDKA DMDVETFYGG ILAAIVVNEG ETAPVGAPIG
LLAETEDEIA EAKVRAKGQS ELETSPAATT TSDAAAAAPK VAPPHGQIKI VATPYAKKLA
KQHKVDINKV TGTGAFGRIT PEDVEKAAGL XPKSNPAATA VAAPIPAAAA PAKASPTSFP
DIPGSTVVPF TTMQIAVSKN MMESLSVPTF RVGYPVSTNA LDALYEKVKP KGVTMTALLA
KAAAMALAQH PVVNATCKDG KSFTYNSSIN IAVAVAINGG LITPVLQDAD KLDLYLLSQK
WKELVDKARA KQLQPHEYNS GTFTLSNLGM FGVDRFDAIL PPGQGAVMAV GASKPTVVSD
SEGFFSVKNK MLVNVTADHR IIYGADLAAF LQTFSKIVEN PESLTM
//
