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Database: UniProt/TrEMBL
Entry: A0A1S4AGV0_TOBAC
LinkDB: A0A1S4AGV0_TOBAC
Original site: A0A1S4AGV0_TOBAC 
ID   A0A1S4AGV0_TOBAC        Unreviewed;       476 AA.
AC   A0A1S4AGV0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   20-DEC-2017, entry version 7.
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=LOC107797489 {ECO:0000313|RefSeq:XP_016475876.1};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Solanales; Solanaceae;
OC   Nicotianoideae; Nicotianeae; Nicotiana.
OX   NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016475876.1};
RN   [1] {ECO:0000313|Proteomes:UP000084051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX   PubMed=24807620; DOI=10.1038/ncomms4833;
RA   Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA   Goepfert S., Peitsch M.C., Ivanov N.V.;
RT   "The tobacco genome sequence and its comparison with those of tomato
RT   and potato.";
RL   Nat. Commun. 5:3833-3833(2014).
RN   [2] {ECO:0000313|RefSeq:XP_016475876.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JUN-2017) 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|RuleBase:RU003423}.
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DR   RefSeq; XP_016475876.1; XM_016620390.1.
DR   GeneID; 107797489; -.
DR   KEGG; nta:107797489; -.
DR   KO; K00627; -.
DR   Proteomes; UP000084051; Genome assembly.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 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   Complete proteome {ECO:0000313|Proteomes:UP000084051};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|RefSeq:XP_016475876.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000084051};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|RefSeq:XP_016475876.1}.
FT   DOMAIN       39    114       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      184    221       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   476 AA;  49725 MW;  D1F56EF605B074F7 CRC64;
     MSSHLLQTTF IPTTPITLRR ASIFPATHLR RTHVIESKIR EIFMPALSST MTEGKIVSWV
     KTEGDKLAKG EAVLVVESDK ADMDVESFYD GYLATIIVPE GGSAPVGSTI ALLAESEEEI
     SLAKAKTPAS ISTSSQETTT PAAAVTEEVV STVAAAAGVS PSDAGPAKMA SAIHPASEGG
     KRVVASPYAK KLAKELGVEL RGLVGSGPNG RIVAKDVEAT VGSTASTPAP VGGVVGTTVA
     KPIGSEPVAP AIELGTTVPF TTMQNAVSRN MVESLAVPTF RVGYTITTNA LDALYKKIKS
     KGVTMTALLA KATALALAKH PVVNSSCRDG KSFTYNSSIN IAVAVAIDGG LITPVLQDAD
     KVDIYSLSRK WKELVDKARA KQLQPHEYTT GTFTLSNLGM FGVDRFDAIL PPGTGAIMAV
     GASHPALVGT KDGRIGMKNQ MQVNVTADHR VIYGADLASF LQTLAQIIED PKDLTL
//
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