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Database: UniProt
Entry: O97227_PLAF7
LinkDB: O97227_PLAF7
Original site: O97227_PLAF7 
ID   O97227_PLAF7            Unreviewed;       448 AA.
AC   O97227;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 151.
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=PF3D7_0303700 {ECO:0000313|EMBL:CAB38991.1};
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329 {ECO:0000313|EMBL:CAB38991.1, ECO:0000313|Proteomes:UP000001450};
RN   [1] {ECO:0000313|EMBL:CAB38991.1, ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=10448855; DOI=10.1038/22964;
RA   Bowman S., Lawson D., Basham D., Brown D., Chillingworth T., Churcher C.M.,
RA   Craig A., Davies R.M., Devlin K., Feltwell T., Gentles S., Gwilliam R.,
RA   Hamlin N., Harris D., Holroyd S., Hornsby T., Horrocks P., Jagels K.,
RA   Jassal B., Kyes S., McLean J., Moule S., Mungall K., Murphy L., Oliver K.,
RA   Quail M.A., Rajandream M.-A., Rutter S., Skelton J., Squares R.,
RA   Squares S., Sulston J.E., Whitehead S., Woodward J.R., Newbold C.,
RA   Barrell B.G.;
RT   "The complete nucleotide sequence of chromosome 3 of Plasmodium
RT   falciparum.";
RL   Nature 400:532-538(1999).
RN   [2] {ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {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., Chan M.S.,
RA   Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA   Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.,
RA   Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA   Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA   Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
RN   [3] {ECO:0000313|EMBL:CAB38991.1, ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368867; DOI=10.1038/nature01095;
RA   Hall N., Pain A., Berriman M., Churcher C., Harris B., Harris D.,
RA   Mungall K., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA   Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA   Christodoulou Z., Clark L., Clark R., Corto C., Cronin A., Davies R.,
RA   Davies P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA   Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA   Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James D.,
RA   Johnson D., Kerhornou A., Knight A., Kontfortov B., Keyes S., Larke N.,
RA   Lawson D., Lennard N., Line A., Maddison M., McLean J., Mooney P.,
RA   Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rajandream M-A., Rutter S., Rutherford K.M., Sanders M.,
RA   Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA   Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.,
RA   Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT   "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL   Nature 419:527-531(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methylpropanoyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-
CC         [protein] = CoA + N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:18865, Rhea:RHEA-COMP:10475,
CC         Rhea:RHEA-COMP:10497, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83142; EC=2.3.1.168;
CC         Evidence={ECO:0000256|ARBA:ARBA00035973};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938,
CC         ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR   EMBL; AL844502; CAB38991.1; -; Genomic_DNA.
DR   RefSeq; XP_001351112.1; XM_001351076.1.
DR   AlphaFoldDB; O97227; -.
DR   SMR; O97227; -.
DR   IntAct; O97227; 3.
DR   STRING; 36329.O97227; -.
DR   SwissPalm; O97227; -.
DR   PaxDb; 5833-PFC0170c; -.
DR   EnsemblProtists; CAB38991; CAB38991; PF3D7_0303700.
DR   GeneID; 814354; -.
DR   KEGG; pfa:PF3D7_0303700; -.
DR   VEuPathDB; PlasmoDB:PF3D7_0303700; -.
DR   HOGENOM; CLU_016733_10_0_1; -.
DR   InParanoid; O97227; -.
DR   OMA; HPCIMAP; -.
DR   OrthoDB; 1399at2759; -.
DR   PhylomeDB; O97227; -.
DR   Reactome; R-PFA-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-PFA-70895; Branched-chain amino acid catabolism.
DR   Proteomes; UP000001450; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:GeneDB.
DR   GO; GO:0016407; F:acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0031405; F:lipoic acid binding; IBA:GO_Central.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
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; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:CAB38991.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:CAB38991.1};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          33..108
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          118..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  50990 MW;  410AE2811DF71FD2 CRC64;
     MFVKNVLNVL RRIEGKSFKG RHYLNTSAIH FKIVKCKLFD IGEGISEVEI TKWHKNEGDQ
     VSEMESLLTV QSDKAAVDIT SKYNGVLVKK YLNENDMLKV GSYFCEIDTD DDIIERDEEE
     VEKEENNKKE EDGESDLSLN DDISNNDYIK ASPGVKRKAK EYKVNLNKVG DYFNKVNISL
     EDLELYYNNV VKNEYSNNIN NNDMDIIEEV SLKGIKLAMC KSMNESLQVP LFHLNEMCII
     NNLIKMRKEY KEQQKNLQTK ETNITITCIL IKLISNVLKE FPILNSKFNF KTNTYTMYKN
     HNISIAVDTP HGLLVPNIKN VQNKNILDIQ KDLLSLRDKA NNMQLDKSDI TNGTITVSNF
     GAISGTFATP IVFDNQACII GIGKMEKKLL LKDESNNLNS LNDILVADTI NFTFGADHRY
     IDGATLAQFS KMLKMNIENC ASLGPLLE
//
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