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Q5ZHN9 (PGPS1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
ORF Names:RCJMB04_35a14
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length557 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
   Technical termComplete proteome
Reference proteome
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 – 2525Mitochondrion Potential
Chain26 – 557532CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
PRO_0000337109

Regions

Domain212 – 23827PLD phosphodiesterase 1
Domain461 – 49434PLD phosphodiesterase 2
Nucleotide binding121 – 1288ATP Potential

Sites

Active site2171 Potential
Active site2191 Potential
Active site2241 Potential

Sequences

Sequence LengthMass (Da)Tools
Q5ZHN9 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 40296640BBAB1B7F

FASTA55763,067
        10         20         30         40         50         60 
MAAAGGAALW RRLAAWLPRG PPGLAALLGR LSDRLSRGRD RRSRRSSWLL LAPLLTPPVP 

        70         80         90        100        110        120 
VITAMPCSLC PEGAHRFQWI RNLVPEFGIS SSHVKVLSSP AEFYELLKVQ IKTAKQRVVM 

       130        140        150        160        170        180 
ASLYLGTGLL EQELVNCLEE TLEKSLQANE SPNLRVSILL DYTRGSRGRK NSRTMLIPLL 

       190        200        210        220        230        240 
QRFPEQVRVS LFHTPNLRGL LKLLIPERFN ETIGLQHIKV YLFDDNVILS GANLSDLYFT 

       250        260        270        280        290        300 
NRQDRYVLLQ DSPEIADFFT ELVDAIGDVS LQLQQDDTVQ MMEGMVHPYQ GDKVRYCEIA 

       310        320        330        340        350        360 
NQRVMEVIDS ARTRQELLHA KTFHSSQQGS SMLPQHDSEA SEGLKPEPDT WIYPLIQMKP 

       370        380        390        400        410        420 
FGIQIDEMVT ETLLTEAERD AKIYLTTGYF NLTQAYMDLI LGTRAEYRIL LASPEVNGFF 

       430        440        450        460        470        480 
GAKGVAGAIP SAYVYIEHQF YNEVCCLHQQ ERVQLQEYSR AGWTFHAKGL WLYLAGSSLP 

       490        500        510        520        530        540 
CLTLIGSPNF GYRSVHRDLE AQVAIVTENK ALQQQLHQEQ EQLYLCSGVV SSSTFEQPSR 

       550 
HVKLWVKLVT PLIKNFF 

« Hide

References

[1]"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis."
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.
Genome Biol. 6:R6.1-R6.9(2005) [PubMed: 15642098] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: CB.
Tissue: Bursa of Fabricius.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ721095 mRNA. Translation: CAG32754.1.
IPIIPI00586398.
RefSeqNP_001008463.1. NM_001008463.1.
UniGeneGga.22573.

3D structure databases

ProteinModelPortalQ5ZHN9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5ZHN9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000011630; ENSGALP00000011616; ENSGALG00000007181.
GeneID422087.
KEGGgga:422087.

Organism-specific databases

CTD9489.

Phylogenomic databases

eggNOGveNOG13078.
GeneTreeENSGT00390000002373.
HOGENOMHBG737293.
HOVERGENHBG057228.
InParanoidQ5ZHN9.
OMARQDRYVL.
OrthoDBEOG4HDSTM.
PhylomeDBQ5ZHN9.

Family and domain databases

InterProIPR016270. PLipase-D_PtdSer-synthase-type.
IPR001736. PLipase_D/transphosphatidylase.
[Graphical view]
KOK00995.
PANTHERPTHR12586. PTHR12586. 1 hit.
PIRSFPIRSF000850. Phospholipase_D_PSS. 1 hit.
PROSITEPS50035. PLD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGPS1_CHICK
AccessionPrimary (citable) accession number: Q5ZHN9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 23, 2004
Last modified: November 16, 2011
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families