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Database: UniProt
Entry: A0A218VZL3_PUNGR
LinkDB: A0A218VZL3_PUNGR
Original site: A0A218VZL3_PUNGR 
ID   A0A218VZL3_PUNGR        Unreviewed;       467 AA.
AC   A0A218VZL3;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   05-JUN-2019, entry version 8.
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=CDL15_Pgr015167 {ECO:0000313|EMBL:OWM65743.1};
OS   Punica granatum (Pomegranate).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Myrtales; Lythraceae; Punica.
OX   NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM65743.1};
RN   [1] {ECO:0000313|EMBL:OWM65743.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Fresh leaf {ECO:0000313|EMBL:OWM65743.1};
RA   Xu C.;
RT   "The pomegranate genome and the genomics of punicalagin
RT   biosynthesis.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OWM65743.1}.
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DR   EMBL; MTKT01005556; OWM65743.1; -; Genomic_DNA.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
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; IPR023213; CAT-like_dom_sf.
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   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN       38    113       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      184    221       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION      123    177       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A218VZL3}.
FT   COMPBIAS    129    143       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A218VZL3}.
SQ   SEQUENCE   467 AA;  48539 MW;  989FDB3B8E525884 CRC64;
     MAHLLKTTFI SSSPALRPRR IPGHRAGRVS THPVQAKIRE IFMPALSSTM TEGKIVSWVK
     SEGDKLSKGE SVVVVESDKA DMDVETFYDG YLAAIVVEEG GVAPVGSAIA LLAESEEEIA
     EAKFKAGSSG LPSSDQSAAP AAQETVPENA GPATPPPQAA KATAAAASAG SAVHPASEGG
     KRIVASPYAK KLAKELKVEL GRIVGSGPNG RIVAKDIEAA AADLAVAAAP APGSAAPPAA
     AAVELGTVVP FTTMQGAVSR NMVESLSVPT FRVGYTITTD ALDALYKKIK SKGVTMTALL
     AKATALALVK HPVVNSSCRD GKSFTYNSNI NIAVAVAMDG GLITPVLQDA DKVDIYSLSR
     KWKELVDKAR AKQLQPHEYN TGTFTLSNLG IFGVDRFDAI LPPGTGAIMA VGASQPTVVA
     SKDGRIGMKN QMQVNVTADH RVIYGADLAS FLQTLAKIID DPKDLTF
//
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