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Database: UniProt/TrEMBL
Entry: Q8IJJ4_PLAF7
LinkDB: Q8IJJ4_PLAF7
Original site: Q8IJJ4_PLAF7 
ID   Q8IJJ4_PLAF7            Unreviewed;       640 AA.
AC   Q8IJJ4;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 2.
DT   27-SEP-2017, entry version 104.
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=PF10_0407 {ECO:0000313|EMBL:AAN35399.2}, PF3D7_1020800
GN   {ECO:0000313|EMBL:CZT98463.1};
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329 {ECO:0000313|EMBL:AAN35399.2, ECO:0000313|Proteomes:UP000001450};
RN   [1] {ECO:0000313|EMBL:AAN35399.2, ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D7 {ECO:0000313|EMBL:AAN35399.2}, and Isolate 3D7
RC   {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.,
RA   Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S.,
RA   Chan M.S., Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S.,
RA   Pertea M., Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B.,
RA   Martin D.M., Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A.,
RA   McFadden G.I., Cummings L.M., Subramanian G.M., Mungall C.,
RA   Venter J.C., Carucci D.J., Hoffman S.L., Newbold C., Davis R.W.,
RA   Fraser C.M., Barrell B.;
RT   "Genome sequence of the human malaria parasite Plasmodium
RT   falciparum.";
RL   Nature 419:498-511(2002).
RN   [2] {ECO:0000313|EMBL:AAN35399.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=3D7 {ECO:0000313|EMBL:CZT98463.1};
RG   P. falciparum Genome Sequencing Consortium;
RA   Aslett M., Brunk B., Gardner M., Berriman M.;
RL   Submitted (JUL-2009) 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}.
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DR   EMBL; AE014185; AAN35399.2; -; Genomic_DNA.
DR   EMBL; LN999944; CZT98463.1; -; Genomic_DNA.
DR   RefSeq; XP_001347486.2; XM_001347450.2.
DR   EnsemblProtists; CZT98463; CZT98463; PF3D7_1020800.
DR   GeneDB; PF3D7_1020800.1:pep; -.
DR   GeneID; 810359; -.
DR   KEGG; pfa:PF10_0407; -.
DR   EuPathDB; PlasmoDB:PF3D7_1020800; -.
DR   HOGENOM; HOG000284461; -.
DR   InParanoid; Q8IJJ4; -.
DR   KO; K00627; -.
DR   OMA; KAVARNM; -.
DR   Reactome; R-PFA-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-PFA-70268; Pyruvate metabolism.
DR   Proteomes; UP000001450; Chromosome 10.
DR   GO; GO:0020011; C:apicoplast; IDA:GeneDB.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IDA:GeneDB.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IC:GeneDB.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; TAS:GeneDB.
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; IPR004167; E3-bd.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:AAN35399.2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001450};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:AAN35399.2}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    640       Dihydrolipoamide acetyltransferase
FT                                component of pyruvate dehydrogenase
FT                                complex. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010976645.
FT   DOMAIN       52    127       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      182    257       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   640 AA;  73890 MW;  185718D379E16CBC CRC64;
     MLYNLIILIF YLRFSKCISK NNNYGYINFG TFSNVVNNSN NLRNRKNVVF SKIEIKMPAL
     SSTMTTGKIV KWNKNIGDYV NLGDIIMTVE SDKADMDVEA FDEGFLRVKR LEDGCEANVG
     DVLGVLTTEE NENMDEKKYN DGDINKTENE IKVLNPDKDK SEQIIKEDIH FVKKHINDDV
     NEEKIFIPFI KCKKKKAKIN KWLKNENDFV KKNDLLLYVE DDKSTIEVES PYSGIIKKLL
     VKEGQFVDLD KEVAIISITE EKDNEKEKIE EPFKNKEDEE INRDNILIHY INKIKKSEEG
     RKFLKNLSEQ EEKTLEERLK LNYEKYNKIS NDLFRSSEST KDYVLKEKEN ESQYEMVLPS
     ASELMRQNKL NPKDITNRKT PNRITYEDVD AFLNGHKNNS TNVTYCEKPK VETIEYGDPK
     TVDMTNIQKS IKNNMMLTLT VPVFRVTHLI KTNELLKLYE KVKQKISMSV IINKCVSSVL
     LNHPLIYSTY IDKDNGKILY NKDVNIGNAL GLPDSLLTPV LKKVDKKDIY TLANEWKILV
     EKGKNGLLSS NDMTGSNFYI SNLGMFNTYQ FDAILPKNSS CILSIGTNIG SIDNLEDLKI
     QKGMMMTLTC DHRHIYGSHA AAFMNDLSKF IEKDIMKIFL
//
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