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Q39639 (PLSB_CUCSA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glycerol-3-phosphate acyltransferase, chloroplastic

Short name=GPAT
EC=2.3.1.15
OrganismCucumis sativus (Cucumber)
Taxonomic identifier3659 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCucumis

Protein attributes

Sequence length470 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

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.

Sequence similarities

Belongs to the GPAT/DAPAT family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   Molecular functionAcyltransferase
Transferase
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 – 101101Chloroplast By similarity
Chain102 – 470369Glycerol-3-phosphate acyltransferase, chloroplastic
PRO_0000024697

Regions

Motif240 – 2456HXXXXD motif

Sequences

Sequence LengthMass (Da)Tools
Q39639 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: AF60144E19D2B39B

FASTA47051,876
        10         20         30         40         50         60 
MFILSAVSSS SSSSSSVPSS LPPFSLSPSI SLSFSRVSLP PSSSSSSSSL KLFLPLSLHF 

        70         80         90        100        110        120 
TPPKLSSPHS FLRFSASRAM AELIQDKESA HTPSTTDVTR NDPPHSRAFL DLRSEEELLS 

       130        140        150        160        170        180 
CIRRETEAGK LPSNVAAGME ELYQNYKNAV FESGNPKADE IVLSNMTVAL DRILLDVEDP 

       190        200        210        220        230        240 
FMFSPHHKAI REPFDYYTFG QNYVRPLIDF ENSFVGNLSL FKDIEEKLHQ GHNVVLISNH 

       250        260        270        280        290        300 
QTEADPAIIS LLLEKTNPYI AENMIYVAGD RVIADPLCKP FSIGRNLICV YSKKHMLDIP 

       310        320        330        340        350        360 
ELAETKRKAN TRSLKEMALL LRGGSQLIWI APSGGRDRPD PSTGEWYPAP FDASSVDNMR 

       370        380        390        400        410        420 
RLLQHSGAPG HLYPLALLCY DIMPPPSQVE IEIGEKRVIS FNGTGLSVGP EISFDEIAAS 

       430        440        450        460        470 
RDNPDEVREA YSKALYDSVA KQYNVLKAAI DGKQELEASV ADVSLSQPWI 

« Hide

References

[1]"Nucleotide sequence of acyl-acyl carrier protein: glycerol-3-phosphate acyltransferase from cucumber."
Johnson T.C., Schneider J.C., Somerville C.
Plant Physiol. 99:771-772(1992) [PubMed: 16668954] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M80571 mRNA. Translation: AAA33122.1.
PIRT10193.

3D structure databases

ProteinModelPortalQ39639.
SMRQ39639. Positions 105-469.
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_CUCSA
AccessionPrimary (citable) accession number: Q39639
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: May 31, 2011
This is version 58 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