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Information on EC 2.7.7.41 - phosphatidate cytidylyltransferase and Organism(s) Plasmodium falciparum

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Plasmodium falciparum
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Word Map
The taxonomic range for the selected organisms is: Plasmodium falciparum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
cdp-diacylglycerol synthase, cdp-dg, phosphatidate cytidylyltransferase, tam41, cdp-dag synthase, tamm41, cdp-diglyceride synthetase, ctp:phosphatidate cytidylyltransferase, cdp-dg synthase, tbcds, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CDP-DAG synthase
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-
-
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CDP-DG
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-
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CDP-DG synthetase
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-
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CDP-diacylglyceride synthetase
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CDP-diacylglycerol synthase
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CDP-diglyceride pyrophosphorylase
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-
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CDP-diglyceride synthetase
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-
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CDPdiglyceride pyrophosphorylase
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-
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CTP-diacylglycerol synthetase
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-
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CTP:1,2-diacylglycerophosphate-cytidyl transferase
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CTP:phosphatidate cytidylyltransferase
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cytidine diphosphoglyceride pyrophosphorylase
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cytidylyltransferase, phosphatidate
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DAG synthetase
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phosphatidate cytidyltransferase
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phosphatidic acid cytidylyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
CTP:phosphatidate cytidylyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9067-83-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
show the reaction diagram
the enzyme catalyzes the synthesis of CDPdiacylglycerol, an obligatory intermediate compound in the biosynthesis of the major anionic and zwitterionic phospholipids
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-
?
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.62
calculated from nucleotide sequence for full-length enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the enzyme is only weakly transcribed in ring stages, while major transcription occurs in the trophozoite and schizont stages
Manually annotated by BRENDA team
the enzyme is only weakly transcribed in ring stages, while major transcription occurs in the trophozoite and schizont stages
Manually annotated by BRENDA team
the enzyme is only weakly transcribed in ring stages, while major transcription occurs in the trophozoite and schizont stages
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
peripheral membrane protein that is trafficked outside the parasite to the parasitophorous vacuole
Manually annotated by BRENDA team
peripheral membrane protein that is trafficked outside the parasite to the parasitophorous vacuole
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme can substitute for the corresponding enzyme in Plasmodium knowlesi. Both the C-terminal cytidylyltransferase domain and the N-terminal extension are essential to Plasmodium spp.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9NIH5_PLAFA
667
7
78004
TrEMBL
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the 78 kDa predicted protein is recovered as a 50 kDa conserved C-terminal cytidylyltransferase domain C-CDS and a 28 kDa fragment that corresponds to the long hydrophilic asparagine-rich N-terminal extension N-CDS. The two fragments are the processed forms of the 78 kDa pro-form that is encoded from a single transcript with no alternate translation start site for C-CDS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Martin, D.; Gannoun-Zaki, L.; Bonnefoy, S.; Eldin, P.; Wengelnik, K.; Vial, H.
Characterization of Plasmodium falciparum CDP-diacylglycerol synthase, a proteolytically cleaved enzyme
Mol. Biochem. Parasitol.
110
93-105
2000
Plasmodium falciparum (Q9NIH5), Plasmodium falciparum
Manually annotated by BRENDA team
Shastri, S.; Zeeman, A.M.; Berry, L.; Verburgh, R.J.; Braun-Breton, C.; Thomas, A.W.; Gannoun-Zaki, L.; Kocken, C.H.; Vial, H.J.
Plasmodium CDP-DAG synthase: an atypical gene with an essential N-terminal extension
Int. J. Parasitol.
40
1257-1268
2010
Plasmodium falciparum (Q8ILZ6), Plasmodium falciparum
Manually annotated by BRENDA team