(data stored in SCRATCH zone)

SWISSPROT: Q8IB37_PLAF7

ID   Q8IB37_PLAF7            Unreviewed;       661 AA.
AC   Q8IB37;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   11-DEC-2019, entry version 99.
DE   RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000256|RuleBase:RU365024};
DE            EC=2.7.8.5 {ECO:0000256|RuleBase:RU365024};
GN   ORFNames=PF3D7_0820200 {ECO:0000313|EMBL:CAD51172.1};
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329 {ECO:0000313|EMBL:CAD51172.1, ECO:0000313|Proteomes:UP000001450};
RN   [1] {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.D.,
RA   Eisen J.A., Rutherford K.M., 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.A.,
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.G.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
RN   [2] {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.M., Harris B., Harris D.,
RA   Mungall K.L., 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., Corton C., Cronin A., Davies R.M.,
RA   Davis 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 K.D.,
RA   Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes 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.R.,
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   -!- FUNCTION: Functions in the biosynthesis of the anionic phospholipids
CC       phosphatidylglycerol and cardiolipin. {ECO:0000256|RuleBase:RU365024}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-
CC         diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP +
CC         H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5;
CC         Evidence={ECO:0000256|RuleBase:RU365024};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC       phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC       {ECO:0000256|RuleBase:RU365024}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU365024}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-II
CC       family. {ECO:0000256|RuleBase:RU365024}.
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DR   EMBL; AL844507; CAD51172.1; -; Genomic_DNA.
DR   RefSeq; XP_001349323.1; XM_001349287.1.
DR   SMR; Q8IB37; -.
DR   EnsemblProtists; CAD51172; CAD51172; PF3D7_0820200.
DR   GeneDB; PF3D7_0820200.1:pep; -.
DR   GeneID; 2655340; -.
DR   KEGG; pfa:PF3D7_0820200; -.
DR   EuPathDB; PlasmoDB:PF3D7_0820200; -.
DR   HOGENOM; HOG000282650; -.
DR   InParanoid; Q8IB37; -.
DR   KO; K00995; -.
DR   OMA; FITKNIV; -.
DR   PhylomeDB; Q8IB37; -.
DR   BioCyc; PLASMO:MAL8P1.58-MONOMER; -.
DR   UniPathway; UPA00084; UER00503.
DR   Proteomes; UP000001450; Chromosome 8.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; ISS:GeneDB.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; ISS:GeneDB.
DR   GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; ISS:GeneDB.
DR   InterPro; IPR016270; PGS1.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR12586; PTHR12586; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   PROSITE; PS50035; PLD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8IB37.
DR   SWISS-2DPAGE; Q8IB37.
KW   ATP-binding {ECO:0000256|RuleBase:RU365024};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU365024};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU365024};
KW   Mitochondrion {ECO:0000256|RuleBase:RU365024};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU365024};
KW   Phospholipid biosynthesis {ECO:0000256|RuleBase:RU365024};
KW   Phospholipid metabolism {ECO:0000256|RuleBase:RU365024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW   Transferase {ECO:0000256|RuleBase:RU365024, ECO:0000313|EMBL:CAD51172.1}.
FT   DOMAIN          126..152
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          514..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   661 AA;  78063 MW;  2150CCEEFE7B92F4 CRC64;
     MALKFVIHEP KAKLLFTPKE FFNTLNDIFK NSQNRIVISC LYMGIGELEK ELIDSIKKNV
     NIKDLKVDIL LDRQRGTRLE GKFNESSVSI LSELFKCSDN INISLFHNPL LGPILYNILP
     PRANEAIGVM HMKIYIGDNI LMLSGANLSD SYLRNRQDRY FVIENKFLAD SIHNIINTIQ
     GMSFTLNRDL TIKWENDLMN PLIDAYVFRE QYYRRIRFML QGIQKHISQY NKNYSYNNYY
     KNIKNDPIND KTYIYNNQNN NKYSYTSNEF RMLNSFSTDI FDKDTYNNKN QKNNHKKENM
     ETHTLLDTNH GTCDSTINLL NNNQNENHTN NLFTYLNEKD EFFYPLFEKN KSILVLELSL
     QCGFSIPPIY DETDMLENLL KNIEKYDQSL VISSGYLNFP MNFLKLIRNI YINVMQKKNG
     ILQLITASPC ANSFYKSKGI SYYIPSSYSA MANVCIEYIT KNLTNFLKKV NGQNVSEQND
     ISNQKIYIEY YKPSWTFHSK GIWIMDNMKS MKNVSNDNDN DNDNNNNDNN NNNNINNNEF
     HSAKKYEQNV NNSPNVKNNL NKSEYFNNEN FDKNIDEEND YYDNLPWCTV IGSSNYGYRA
     KYRDLEMSFI IKTNDYNLRC QLKKELNIIY ESSHFVQVDE LKLRYAFWLK FLVKYIFKWL
     L
//

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