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Protein

Phosphatidate cytidylyltransferase 1

Gene

CDS1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in the synthesis of minor phospholipids and in modulation of IP3-mediated signal transduction.1 Publication

Catalytic activityi

CTP + phosphatidate = diphosphate + CDP-diacylglycerol.1 Publication

Cofactori

Mg2+By similarityNote: Requires a divalent cation for activity.By similarity

Pathway: CDP-diacylglycerol biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate.1 Publication
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Probable glycerol-3-phosphate acyltransferase 2 (GPAT2), Glycerol-3-phosphate acyltransferase, chloroplastic (ATS1), Glycerol-3-phosphate acyltransferase 1 (GPAT1), Probable glycerol-3-phosphate acyltransferase 3 (GPAT3), Glycerol-3-phosphate acyltransferase 7 (GPAT7), Probable glycerol-3-phosphate acyltransferase 8 (GPAT8), Glycerol-3-phosphate acyltransferase 5 (GPAT5)
  2. 1-acyl-sn-glycerol-3-phosphate acyltransferase 3 (LPAT3), 1-acyl-sn-glycerol-3-phosphate acyltransferase 2 (LPAT2), 1-acyl-sn-glycerol-3-phosphate acyltransferase 1, chloroplastic (LPAT1), Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 5 (LPAT5), Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 4 (LPAT4)
  3. Phosphatidate cytidylyltransferase 1 (CDS1), Phosphatidate cytidylyltransferase 3 (CDS3), Phosphatidate cytidylyltransferase 4, chloroplastic (CDS4), Phosphatidate cytidylyltransferase 2 (CDS2), Phosphatidate cytidylyltransferase 5, chloroplastic (CDS5), Phosphatidate cytidylyltransferase (CDS2), Phosphatidate cytidylyltransferase (CDS2)
This subpathway is part of the pathway CDP-diacylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate, the pathway CDP-diacylglycerol biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

  • phosphatidate cytidylyltransferase activity Source: TAIR

GO - Biological processi

  • CDP-diacylglycerol biosynthetic process Source: GO_Central
  • developmental vegetative growth Source: TAIR
  • phosphatidylglycerol biosynthetic process Source: GO_Central
  • phospholipid biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciMetaCyc:AT1G62430-MONOMER.
ReactomeiREACT_348459. Synthesis of PG.
REACT_354726. Synthesis of PI.
UniPathwayiUPA00557; UER00614.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidate cytidylyltransferase 11 Publication (EC:2.7.7.411 Publication)
Alternative name(s):
CDP-DAG synthase 1
CDP-DG synthase 1
CDP-diacylglycerol synthase 1
Short name:
CDS1
CDP-diglyceride pyrophosphorylase 1
CDP-diglyceride synthase 1
CTP:phosphatidate cytidylyltransferase 1
Gene namesi
Name:CDS11 Publication
Ordered Locus Names:At1g62430Imported
ORF Names:F24O1.17Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G62430.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei60 – 8021Helical; Name=1Sequence AnalysisAdd
BLAST
Transmembranei102 – 12221Helical; Name=2Sequence AnalysisAdd
BLAST
Transmembranei149 – 16921Helical; Name=3Sequence AnalysisAdd
BLAST
Transmembranei183 – 20321Helical; Name=4Sequence AnalysisAdd
BLAST
Transmembranei206 – 22621Helical; Name=5Sequence AnalysisAdd
BLAST
Transmembranei246 – 26621Helical; Name=6Sequence AnalysisAdd
BLAST
Transmembranei321 – 34121Helical; Name=7Sequence AnalysisAdd
BLAST
Transmembranei369 – 38921Helical; Name=8Sequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: TAIR
  • endoplasmic reticulum membrane Source: GO_Central
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 421421Phosphatidate cytidylyltransferase 1PRO_0000090723Add
BLAST

Proteomic databases

PaxDbiO04928.
PRIDEiO04928.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G62430.1.

Structurei

3D structure databases

ProteinModelPortaliO04928.
SMRiO04928. Positions 193-379.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CDS family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0575.
HOGENOMiHOG000209582.
InParanoidiO04928.
KOiK00981.
OMAiVHMTLLL.
PhylomeDBiO04928.

Family and domain databases

InterProiIPR000374. PC_trans.
IPR016720. PC_Trfase_euk.
[Graphical view]
PIRSFiPIRSF018269. PC_trans_euk. 1 hit.
PROSITEiPS01315. CDS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O04928-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEENVTSSP STPVHRLRHR RRSNEVVTDG DKVNASPLLV NDRNKYKSFM
60 70 80 90 100
VRTYSTLWMI GGFVLVVYMG HLYITAMVVV IQIFMAKELF NLLRKAPEDK
110 120 130 140 150
CLPYIKQLNW HFFFTAMLFV YGRILSQRLA NTMTADQFFY RLVSGLIKYH
160 170 180 190 200
MAICYLLYII GFMWFILTLK KKMYKYQFGQ YAWTHMILIV VFTQSSFTVA
210 220 230 240 250
NIFEGIFWFL LPASLIIIND IFAYIFGFFF GRTPLIKLSP KKTWEGFIGA
260 270 280 290 300
SVTTIISAFV LANILGRFPW LTCPRQDLST GWLQCDADPL FKPEPFALPA
310 320 330 340 350
WIPEWFPWKE MTILPVQWHA LCLGLFASII APFGGFFASG FKRAFKIKDF
360 370 380 390 400
GDSIPGHGGI TDRMDCQMVM AVFAYIYLQS FIVSQSVSVD KILDQILTNL
410 420
TFEEQQALFV KLGQMLKDKL S
Length:421
Mass (Da):48,660
Last modified:July 1, 1997 - v1
Checksum:i96D238DB4B913AA3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94306 mRNA. Translation: CAA63969.1.
AC003113 Genomic DNA. Translation: AAF70845.1.
CP002684 Genomic DNA. Translation: AEE33967.1.
PIRiT01455.
RefSeqiNP_176433.2. NM_104923.3.
UniGeneiAt.23658.

Genome annotation databases

EnsemblPlantsiAT1G62430.1; AT1G62430.1; AT1G62430.
GeneIDi842541.
KEGGiath:AT1G62430.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94306 mRNA. Translation: CAA63969.1.
AC003113 Genomic DNA. Translation: AAF70845.1.
CP002684 Genomic DNA. Translation: AEE33967.1.
PIRiT01455.
RefSeqiNP_176433.2. NM_104923.3.
UniGeneiAt.23658.

3D structure databases

ProteinModelPortaliO04928.
SMRiO04928. Positions 193-379.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G62430.1.

Proteomic databases

PaxDbiO04928.
PRIDEiO04928.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G62430.1; AT1G62430.1; AT1G62430.
GeneIDi842541.
KEGGiath:AT1G62430.

Organism-specific databases

TAIRiAT1G62430.

Phylogenomic databases

eggNOGiCOG0575.
HOGENOMiHOG000209582.
InParanoidiO04928.
KOiK00981.
OMAiVHMTLLL.
PhylomeDBiO04928.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00614.
BioCyciMetaCyc:AT1G62430-MONOMER.
ReactomeiREACT_348459. Synthesis of PG.
REACT_354726. Synthesis of PI.

Miscellaneous databases

PROiO04928.

Family and domain databases

InterProiIPR000374. PC_trans.
IPR016720. PC_Trfase_euk.
[Graphical view]
PIRSFiPIRSF018269. PC_trans_euk. 1 hit.
PROSITEiPS01315. CDS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complementary DNAs encoding eukaryotic-type cytidine-5'-diphosphate-diacylglycerol synthases of two plant species."
    Kopka J., Ludewig M., Mueller-Roeber B.
    Plant Physiol. 113:997-1002(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. C24.
    Tissue: Flower and Silique.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Two closely related genes of Arabidopsis encode plastidial cytidinediphosphate diacylglycerol synthases essential for photoautotrophic growth."
    Haselier A., Akbari H., Weth A., Baumgartner W., Frentzen M.
    Plant Physiol. 153:1372-1384(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, GENE FAMILY, NOMENCLATURE.
  5. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCDS1_ARATH
AccessioniPrimary (citable) accession number: O04928
Secondary accession number(s): O48808
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: June 24, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.