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Reviewed, UniProtKB/Swiss-Prot P79001 (PGPS1_SACPS)

Last modified June 16, 2009. Version 45. 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
    EC=2.7.8.5
Alternative name(s):
    Phosphatidylglycerophosphate synthase
      Short name=PGP synthase
Gene names
Name: PGS1
Synonyms: PEL1, YCLUN3W
OrganismSaccharomyces pastorianus (Lager yeast) (Saccharomyces carlsbergensis)
Taxonomic identifier27292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length521 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Essential for the viability of mitochondrial petite mutant. Catalyzes the committed step to the synthesis of the acidic phospholipids By similarity.

Catalytic activity

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

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
   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

Chain1 – 521521CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
PRO_0000056826

Regions

Domain177 – 20327PLD phosphodiesterase 1
Domain419 – 45739PLD phosphodiesterase 2
Nucleotide binding91 – 988ATP Potential

Sites

Active site1821 Potential
Active site1841 Potential
Active site1891 Potential

Sequences

Sequence LengthMass (Da)Tools
P79001-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 1E28ABDDB2231302

FASTA52159,354
        10         20         30         40         50         60 
MTTRLLQLTR PHYRLLSSPF RKSSIIQRQM SASSPSPANS YLNMITKSLQ HNLQTWFHFE 

        70         80         90        100        110        120 
PNEIDIIESP SHFYDLLKSK ISSSQKRIFI ASLYLGKSET ELIDCISQAL SKNPDLKVSF 

       130        140        150        160        170        180 
LLDGLRGTRE LPSTCSATLL SSLVAKYGSE RVDCRLYKTP AYHGWKKIVV PKRFNEGLGL 

       190        200        210        220        230        240 
QHMKIYGFDN EIILSGANLS NDYFTNRQDR YYLFKSANFA NYYFKLHQLI SSFSYQIVKP 

       250        260        270        280        290        300 
KVAGNVNIIW PDSNPTIEPM KNKRKFLREA SQLLENFLQI SKHNQPISPP GQFSTIVYPI 

       310        320        330        340        350        360 
SQFTPLFPKY NDKSTEKSTI LSLLSNIKNT SISWTFTAGY FNILPEIKAN LLATPVTEAN 

       370        380        390        400        410        420 
VITASPFANG FYQSKGVSSN LPGAYLYLSK KFLQDVSRYN KDQAITLREW QRGVVNKPNG 

       430        440        450        460        470        480 
WSYHAKGIWI SSRDNNDSDS WKPFITVIGS SNYTRRAYSL DLESNALIIT KDEELRNKMK 

       490        500        510        520 
GELNDLLQYT KPVTLEDFKS DPERHVGTGV KIATSVLGKK L 

« Hide

References

[1]Andersen T., Nilsson-Tillgren T.
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

Z86109 Genomic DNA. Translation: CAB06796.1.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA2.7.8.5. 3401.

Family and domain databases

InterProIPR016270. PLipase-D_PtdSer-synthase-type.
IPR001736. PLipase_D/transphosphatidylase.
[Graphical view]
PfamPF00614. PLDc. 2 hits.
[Graphical view]
PIRSFPIRSF000850. Phospholipase_D_PSS. 1 hit.
SMARTSM00155. PLDc. 2 hits.
[Graphical view]
PROSITEPS50035. PLD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGPS1_SACPS
AccessionPrimary (citable) accession number: P79001
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: June 16, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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