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Reviewed, UniProtKB/Swiss-Prot Q5R8K7 (PGPS1_PONAB)

Last modified January 19, 2010. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
    EC=2.7.8.5
Alternative name(s):
    Phosphatidylglycerophosphate synthase 1
      Short name=PGP synthase 1
Gene names
Name: PGS1
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length556 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin By similarity.

Catalytic activity

CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate.

Enzyme regulation

Activated by calcium and magnesium and inhibited by other bivalent cations By similarity.

Pathway

Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the CDP-alcohol phosphatidyltransferase class-II family.

Contains 2 PLD phosphodiesterase domains.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentMitochondrion
   DomainRepeat
Transit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionTransferase
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Potential
Chain29 – 556528CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
PRO_0000337108

Regions

Domain215 – 24127PLD phosphodiesterase 1
Domain460 – 49334PLD phosphodiesterase 2
Nucleotide binding124 – 1318ATP Potential

Sites

Active site2201 Potential
Active site2221 Potential
Active site2271 Potential

Sequences

Sequence LengthMass (Da)Tools
Q5R8K7-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 9F49F37C7152AF8C

FASTA55662,701
        10         20         30         40         50         60 
MAVAAAAAAG PVFWRRLLGL LPGRPGLAAL LGRLSDRLGR NRDRQRRRSP WLLLAPLLSP 

        70         80         90        100        110        120 
AVPQVTSPPC CLCPEGVHRF QWIRNLVPEF GVSSSHVRVL SSPAESFELM KGQIRVAKRR 

       130        140        150        160        170        180 
VVMASLYLGT GPLEQELVDC LESTLEKSLQ AKFPSNLKVS ILLDFTRGSR GRKNSRTMLL 

       190        200        210        220        230        240 
PLPQRFPEQV RVSLFHTPHL RGLLRLLIPE RFNETIGLQH IKVYLFDNSV ILSGANLSDS 

       250        260        270        280        290        300 
YFTNRQDRYV FLQDCAEIAD FFTELVDAVG DVSLQLQGDD TVQVVDGMVH PYKGDRTEYC 

       310        320        330        340        350        360 
KAANKRVMDV INSARTRQQM LHAQTFHSNS LLTQEDAAAA GDRRPAPDTW IYPLIQMKPF 

       370        380        390        400        410        420 
EIQIDEIVTE TLLTEAERGA KVYLTTGYFN LTQAYMDLVL GTRAEYQILL ASPEVNGFFG 

       430        440        450        460        470        480 
AKGVVGAIPA AYVHIERQFY SEVCSLGQQE RVQLQEYWRR GWTFHAKGLW LYLAGSSLPC 

       490        500        510        520        530        540 
LTLIGSPNFG YRSVHRDLEA QIAIVTENEA LQQQLHQEQE QLYLRSGVVS SATFEQPSRQ 

       550 
VKLWVKMVTP LIKNFF 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR859745 mRNA. Translation: CAH91903.1.
RefSeqNP_001126101.1.
UniGenePab.13048

3D structure databases

SMRQ5R8K7. Positions 97-268.
ModBaseSearch...

Genome annotation databases

GeneID100173056.

Organism-specific databases

CTD100173056.

Phylogenomic databases

HOVERGENQ5R8K7.
InParanoidQ5R8K7.

Family and domain databases

InterProIPR016270. PLipase-D_PtdSer-synthase-type.
IPR001736. PLipase_D/transphosphatidylase.
[Graphical view]
PIRSFPIRSF000850. Phospholipase_D_PSS. 1 hit.
PROSITEPS50035. PLD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGPS1_PONAB
AccessionPrimary (citable) accession number: Q5R8K7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 21, 2004
Last modified: January 19, 2010
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents