Q9Z2Z7 (PGPS1_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)

Taxonomic identifier

10029 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length	553 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin. Ref.1
Catalytic activity	CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate. Ref.1 Ref.2
Enzyme regulation	Activated by calcium and magnesium and inhibited by other bivalent cations. Ref.2
Pathway	Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Subcellular location	Mitochondrion Ref.2.
Sequence similarities	Belongs to the CDP-alcohol phosphatidyltransferase class-II family. Contains 2 PLD phosphodiesterase domains.
Biophysicochemical properties	Kinetic parameters: KM=288 µM for CDP-diacylglycerol Ref.2 Vmax=13.6 µmol/min/mg enzyme

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Mitochondrion
Domain	Repeat Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Transferase
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from direct assay Ref.1. Source: HGNC
Cellular component	mitochondrion Inferred from mutant phenotype Ref.1. Source: HGNC
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity Inferred from direct assay Ref.1. Source: HGNC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 25	25	Mitochondrion Potential
	Chain	26 – 553	528	CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial		PRO_0000337106
Regions
	Domain	212 – 238	27	PLD phosphodiesterase 1
	Domain	457 – 490	34	PLD phosphodiesterase 2
	Nucleotide binding	121 – 128	8	ATP Potential
Sites
	Active site	217	1	Potential
	Active site	219	1	Potential
	Active site	224	1	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9Z2Z7 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: B5422CF157995A28	FASTA	553	62,369
	10 20 30 40 50 60 MAAPAAGPVF WRRLLGLLPG RPGLAALLGR LSDRLGRSRE RRRRRSPWLL LAPLLSPTVP 70 80 90 100 110 120 QVTSPPCCLC PEGVHRFQWI RNLVPEFGVS SSHVRVLSSP AEFFELLKGQ IKMAKRRVVM 130 140 150 160 170 180 ASLYLGTGPL EQELVDCLES SLEKSLQSKF PSDLKVSILL DFTRGSRGRK NSRTMLLPLL 190 200 210 220 230 240 QRFPEHVRVS LFHTPNLRGL LRLLIPERFN ETIGLQHIKV YLFDNNVVLS GANLSDSYFT 250 260 270 280 290 300 NRQDRYVFLQ DCAEIADFFT ELVDAVGDVS LQLQGDDTVD VVDGMVHPYK GDRAAYCRAA 310 320 330 340 350 360 NKRVMDVIHS ARTRQQLLHA QTFHSDSLLS QEEAAAAGDR RPAPDTWIYP LIQMKPFEIQ 370 380 390 400 410 420 IDEIVTETLL TEAERGAKVF LTTGYFNLTQ AYMDLVLGTR AEYQILLASP EVNGFFGAKG 430 440 450 460 470 480 VAGAIPAAYV HIERQFYGEV CGLGQQDRVQ LQEYWRTGWT FHAKGLWLYL AGSSLPCLTL 490 500 510 520 530 540 IGSPNFGYRS VHRDLEAQIA IVTESRALQQ QLHQEQEQLY LRSSVVTSAT FEQPGRQVKL 550 WVKMVTPLIK NFF

References

[1]

"Isolation of a chinese hamster ovary (CHO) cDNA encoding phosphatidylglycerophosphate (PGP) synthase, expression of which corrects the mitochondrial abnormalities of a PGP synthase-defective mutant of CHO-K1 cells." Kawasaki K., Kuge O., Chang S.-C., Heacock P.N., Rho M., Suzuki K., Nishijima M., Dowhan W. J. Biol. Chem. 274:1828-1834(1999) [PubMed: 9880566] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY. Tissue: Ovary.

[2]

"Purification of phosphatidylglycerophosphate synthase from Chinese hamster ovary cells." Kawasaki K., Kuge O., Yamakawa Y., Nishijima M. Biochem. J. 354:9-15(2001) [PubMed: 11171073] [Abstract] Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB016930 mRNA. Translation: BAA37113.1.
RefSeq	NP_001233637.1. NM_001246708.1.
3D structure databases
ProteinModelPortal	Q9Z2Z7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100689449.
Phylogenomic databases
HOVERGEN	HBG057228.
Family and domain databases
InterPro	IPR016270. PLipase-D_PtdSer-synthase-type. IPR001736. PLipase_D/transphosphatidylase. [Graphical view]
PANTHER	PTHR12586. PTHR12586. 1 hit.
PIRSF	PIRSF000850. Phospholipase_D_PSS. 1 hit.
PROSITE	PS50035. PLD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGPS1_CRIGR

Accession

Primary (citable) accession number: Q9Z2Z7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 1, 1999
Last modified:	January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program