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Reviewed, UniProtKB/Swiss-Prot Q42713 (PLSB_CARTI)

Last modified June 16, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Glycerol-3-phosphate acyltransferase, chloroplastic
      Short name=GPAT
    EC=2.3.1.15
OrganismCarthamus tinctorius (Safflower)
Taxonomic identifier4222 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridscampanulidsAsteralesAsteraceaeCarduoideaeCardueaeCarthamus

Protein attributes

Sequence length463 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 – 9191Chloroplast Potential
Chain92 – 463372Glycerol-3-phosphate acyltransferase, chloroplastic
PRO_0000024695

Regions

Motif229 – 2346HXXXXD motif

Sequences

Sequence LengthMass (Da)Tools
Q42713-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5792E933068A534D

FASTA46350,835
        10         20         30         40         50         60 
MSIFFSPSSP TLFFSTTNAN PRVSPSSSPS SAFTPPLSSS RLRPILRGFP CLAFSAPANA 

        70         80         90        100        110        120 
AHGTAETVHG NKWPSPSSSS SAATQPSAGS DHGHSRTFID ARSEQDLLSG IQRELEAGTL 

       130        140        150        160        170        180 
PKHIAQAMEE LYQNYKNAVL QSAAPHAEDI VLSNMRVAFD RMFLDVKEPF EFSPYHEAIL 

       190        200        210        220        230        240 
EPFNYYMFGQ NYIRPLVNFR ESYVGNVSVF GVMEEQLKQG DKVVLISNHQ TEADPAVIAL 

       250        260        270        280        290        300 
MLETTNPHIS ENIIYVAGDR VITDPLCKPF SMGRNLLCVY SKKHMNDVPE LAEMKKRSNT 

       310        320        330        340        350        360 
RSLKGRMALL LRGGSKIIWI APSGGRDRPD PITNQWFPAP FDATSLDNMR RLVDHAGLVG 

       370        380        390        400        410        420 
HIYPLAILCH DIMPPPLQVE KEIGEKSWIS FHGTGISVAP EINFQEVTAS CGSPEEAKAA 

       430        440        450        460 
YSQALYDSVC EQYKVLHSAV HGGKGLEAST PSVSLSQPLQ FLD 

« Hide

References

[1]"Nucleotide sequence of a cDNA from Carthamus tinctorius encoding a glycerol-3-phosphate acyl transferase."
Bhella R.S., Mackenzie S.L.
Plant Physiol. 106:1713-1714(1994) [PubMed: 7846182] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cotyledon.

Cross-references

Sequence databases

L33841 mRNA. Translation: AAA74319.1.

3D structure databases

HSSPHSSP built from PDB template 1K30 based on UniProtKB P10349.
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.3.1.15. 66868.

Family and domain databases

InterProIPR002123. Acyltransferase.
IPR016222. Glycerol-3-P_O-acyltransferase.
[Graphical view]
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_CARTI
AccessionPrimary (citable) accession number: Q42713
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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