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Reviewed, UniProtKB/Swiss-Prot Q9HDW1 (PGPS1_SCHPO)

Last modified January 19, 2010. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
ORF Names: SPBP18G5.02
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length534 AA.
Sequence statusComplete.
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.

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
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_SPombe

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: GeneDB_SPombe

   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 – 534534CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
PRO_0000350817

Regions

Domain143 – 16927PLD phosphodiesterase 1
Domain421 – 47555PLD phosphodiesterase 2
Nucleotide binding58 – 658ATP Potential

Sites

Active site1481 Potential
Active site1501 Potential
Active site1551 Potential

Sequences

Sequence LengthMass (Da)Tools
Q9HDW1-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 1027C2573F4CDBCD

FASTA53461,429
        10         20         30         40         50         60 
MDEGIEKNIF VNLESQIDGV CPKFYVNVDD IDIIHEPPEF YQRLKKLIKK AQKRIFLSTL 

        70         80         90        100        110        120 
YIGKEERELI NCLSNALSNN PSLHVHILAD QLRCTRESPG CCSASLLMQL KKKFPDRCEI 

       130        140        150        160        170        180 
KLYHTPNLRG LRKQLVPHRF NEGWGLQHMK IYGADDNLII SGANLSRDYF TNRKDRYYLF 

       190        200        210        220        230        240 
SDKGLADFFF KTHFLFSQLS FECIPHLSDS SIQLSSTSPV IPFTLKWNNS CPNPLTNPQE 

       250        260        270        280        290        300 
FRVAASAKIQ QLLQGNREKF LSRNPSKPLS SVYGSELINQ AGDDNNKPFH KYEESAIVYP 

       310        320        330        340        350        360 
LFQCVPILTS DVHSTEEKVL SIIGTLLSRK EVNWTLTAGY FNVYPALRKQ LLKSEGIGEV 

       370        380        390        400        410        420 
IVASQQANGF YRSPGPSKLI PPAYQYIAEQ FLKDSRKKKR NIDVLQWQNK GNTYHAKGKH 

       430        440        450        460        470        480 
YSLSFSIINI FWSTALKSYI FEKFTNTILG FWLSTQHHKH PFLTTIGSSN YTSRSQQLDL 

       490        500        510        520        530 
ESTLVVMTQN EKLKRKFSTE IELIKQHTKP MNTCQLEKVP MYVKALTSLM KKKL 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAC21490.1.
RefSeqNP_595992.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ9HDW1.

Genome annotation databases

GeneID2541243.
GenomeReviewsGene locus pgs1 in contig CU329671_GR.
KEGGspo:SPBP18G5.02.
NMPDRfig|4896.1.peg.1858.

Organism-specific databases

GeneDB_SpombeSPBP18G5.02.

Phylogenomic databases

eggNOGfuNOG07754.
HOGENOMHBG737293.
OMARQDRYVL.
OrthoDBEOG9Z644X.
PhylomeDBQ9HDW1.

Gene expression databases

ArrayExpressQ9HDW1.

Family and domain databases

InterProIPR016270. PLipase-D_PtdSer-synthase-type.
[Graphical view]
PIRSFPIRSF000850. Phospholipase_D_PSS. 1 hit.
PROSITEPS50035. PLD. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGPS1_SCHPO
AccessionPrimary (citable) accession number: Q9HDW1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: March 1, 2001
Last modified: January 19, 2010
This is version 36 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

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

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