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Database: UniProt
Entry: Q7RFX9_PLAYO
LinkDB: Q7RFX9_PLAYO
Original site: Q7RFX9_PLAYO 
ID   Q7RFX9_PLAYO            Unreviewed;       561 AA.
AC   Q7RFX9;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   08-NOV-2023, entry version 110.
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=PY04573 {ECO:0000313|EMBL:EAA16454.1};
OS   Plasmodium yoelii yoelii.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=73239 {ECO:0000313|EMBL:EAA16454.1, ECO:0000313|Proteomes:UP000008553};
RN   [1] {ECO:0000313|EMBL:EAA16454.1, ECO:0000313|Proteomes:UP000008553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17XNL {ECO:0000313|EMBL:EAA16454.1,
RC   ECO:0000313|Proteomes:UP000008553};
RX   PubMed=12368865; DOI=10.1038/nature01099;
RA   Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA   Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA   Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA   Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA   Shoaibi A., Cummings L.M., Florens L., Yates J.R., Raine J.D., Sinden R.E.,
RA   Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W., Vaidya A.B.,
RA   van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA   Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA   Carucci D.J.;
RT   "Genome sequence and comparative analysis of the model rodent malaria
RT   parasite Plasmodium yoelii yoelii.";
RL   Nature 419:512-519(2002).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAA16454.1}.
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DR   EMBL; AABL01001401; EAA16454.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7RFX9; -.
DR   STRING; 73239.Q7RFX9; -.
DR   PaxDb; 73239-Q7RFX9; -.
DR   EnsemblProtists; EAA16454; EAA16454; EAA16454.
DR   InParanoid; Q7RFX9; -.
DR   OMA; AIKNNMM; -.
DR   Proteomes; UP000008553; Unassembled WGS sequence.
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; 2.
DR   Gene3D; 2.40.50.100; -; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like 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; 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; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008553};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU003423};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..561
FT                   /note="Dihydrolipoamide acetyltransferase component of
FT                   pyruvate dehydrogenase complex"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004293885"
FT   DOMAIN          50..125
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          171..247
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          129..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   561 AA;  63458 MW;  0C843A421D4AC7B5 CRC64;
     MMRYFIFFLA FWLNIYKCIN NIKNRNSYGF INLNNNLKLH HKNKHVLYSK VEIKMPALSS
     TMTSGKIVRW NKSVGEFINV GDIIMTVESD KADMDVESFD EGYLRRKLIE EGSEANVGDV
     LGILTTEENE EVANEEAENE KTTDVEMSDV ETTSVETADV ETTDVEGESV EKGIYSPSVQ
     SKKNKVRIAK WLCKENEFVN KSDVIFHIED DKSTIEVDSP YTGIIKTILV KEGELADLEK
     QVATILETNE LENTSMNLSS EADPKTIKEH AQHNQEHGIS HERIVLPSAI ELMKKHKLTP
     EDITHTTIPN RITYEDVNMF LEKKKKIPKV GSDTRVEGGG RVVKLTNIQK SIKNNMMLTL
     NVPVFRITHL IKTCQLLKIY EQVKDKISMS VILNKCVSLA LLKNPLIYST YIDNENGEIL
     YNQNINIGNA LGLNDCLLTP VLKNVDKKDI YTLSTEWKDL VKKGKSGTLS ANEMSGSNFF
     ISNLGMFNTY QFDAILPKNA SCILSIGTNI VSINQFEDLK INKGIMMTLT CDHRHIYGSH
     AAIFMNDLAN VIENSIMDIF L
//
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