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P30706 (PLSB_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 66. 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:
Glycerol-3-phosphate acyltransferase, chloroplastic

Short name=GPAT
EC=2.3.1.15
Gene names
Name:GPAT
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate. The enzyme from chilling-resistant plants discriminates against non-fluid palmitic acid and selects oleic acid whereas the enzyme from sensitive plants accepts both fatty acids. This is an oleate-selective acyltransferase.

Catalytic activity

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.

Subcellular location

Plastidchloroplast stroma.

Domain

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the GPAT/DAPAT family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   Molecular functionAcyltransferase
Transferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast stroma

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglycerol-3-phosphate O-acyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8888Chloroplast Potential
Chain89 – 457369Glycerol-3-phosphate acyltransferase, chloroplastic
PRO_0000024698

Regions

Motif227 – 2326HXXXXD motif

Sequences

Sequence LengthMass (Da)Tools
P30706 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: C50F52102E4C4EB0

FASTA45750,760
        10         20         30         40         50         60 
MTDSFAHCAS HINYRHKMKT MFIFSTPCCS PSTAFFSPFR ASNSKPLRST LSLRSSISSS 

        70         80         90        100        110        120 
SITSTSHCSL AFNIVKHKEK NVVSANMTSS VSSRTFLNAQ NEQDVLSGIK KEVEAGTLPA 

       130        140        150        160        170        180 
SIAAGMEEVY LNYKSAVIKS GDPKANEIVL SNMTALLDRI FLDVKEPFVF EAHHKAKREP 

       190        200        210        220        230        240 
FDYYMFGQNY IRPLVDFETS YVGNMPLFIQ MEEQLKQGHN IILMSNHQSE ADPAIIALLL 

       250        260        270        280        290        300 
EMRLPHIAEN LIYVAGDRVI TVPLCKPFSI GRNLICVYSK KHMLDNPELV DMKRKANTRS 

       310        320        330        340        350        360 
RKEMAMLLRS GSQIIWIAPS GGRDRPVANS GEWAPAPFDS SSVDNMRRLV DHSGPPGHIY 

       370        380        390        400        410        420 
PLAILCHDIM PPPLKVEKEI GEKRIISYHG TGISTAPEIS FSNTTAACEN PEKAKDAYTK 

       430        440        450 
ALYDSVTEQY DVLKSAIHGK KGLQASTPVV SLSQPWK 

« Hide

References

[1]"Purification and cDNA sequencing of an oleate-selective acyl-ACP:sn-glycerol-3-phosphate acyltransferase from pea chloroplasts."
Weber S., Wolter F.-P., Buck F., Frentzen M., Heinz E.
Plant Mol. Biol. 17:1067-1076(1991) [PubMed: 1932680] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 112-134; 310-323 AND 326-345.
Strain: cv. Little Marvel.
Tissue: Seedling.
[2]"Specificities and selectivities of glycerol-3-phosphate acyltransferase and monoacylglycerol-3-phosphate acyltransferase from pea and spinach chloroplasts."
Frentzen M., Heinz E., McKeon T.A., Stumpf P.K.
Eur. J. Biochem. 129:629-636(1983) [PubMed: 6825679] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59041 mRNA. Translation: CAA41769.1.
PIRS18239.

3D structure databases

ProteinModelPortalP30706.
SMRP30706. Positions 93-456.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002123. Acyltransferase.
IPR016222. G3P_O-acylTrfase_chlp.
IPR023083. G3P_O-acylTrfase_N.
[Graphical view]
Gene3DG3DSA:1.10.1200.50. G3P_O-acylTrfase_N. 1 hit.
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFPIRSF000431. Glycerol-3-P_O-acyltransfrase. 1 hit.
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLSB_PEA
AccessionPrimary (citable) accession number: P30706
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: May 31, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families