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
//