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Reviewed, UniProtKB/Swiss-Prot Q43822 (PLSB_PHAVU)

Last modified February 9, 2010. Version 57. 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
Gene names
Name: PLSB
OrganismPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifier3885 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

Protein attributes

Sequence length461 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 – 9696Chloroplast Potential
Chain97 – 461365Glycerol-3-phosphate acyltransferase, chloroplastic
PRO_0000024699

Regions

Motif231 – 2366HXXXXD motif

Sequences

Sequence LengthMass (Da)Tools
Q43822-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: EAC4FC837908B38A

FASTA46150,697
        10         20         30         40         50         60 
MSMTGSSAYY VAHAIPPFLR LSNKTMLLLS TPPTTFFPTS TTPRVTLLSS TSSSSSSSIS 

        70         80         90        100        110        120 
LRSSTAPSPS CSSVTPKDNC LASAKHSPPN MSASVSSRTF LNAQSEQDVF AGIKKEVEAG 

       130        140        150        160        170        180 
SLPANVAAGM EEVYNNYKKA VIQSGDPKAN EIVLSNMIAL LDRVFLDVTD PFVFQPHHKA 

       190        200        210        220        230        240 
KREPFDYYVF GQNYIRPLVD FKNAYVGNMP LFIEMEEKLK QGHNIILMSN HQTEADPAII 

       250        260        270        280        290        300 
SLLLETRLPY IAENLTYVAG DRVITDPLSK PFSIGRNLIC VYSKKHMLDD PALVEMKRTA 

       310        320        330        340        350        360 
NIRALKEMAM LLRNGSQLVW IAPSGGRDRP DAQTREWVPA PFDISSVDNM RRLVEHSGPP 

       370        380        390        400        410        420 
GHVYPLAILC HDIMPPPLKV EKEIGEKRII CFHGAGISVA PAISFSETTA TCENPEKAKE 

       430        440        450        460 
VFSKALYNSV TEQYNVLKSA IQGKKGFEAS TPVVTLSQPW K 

« Hide

References

[1]"Cloning and sequencing of a full-length cDNA coding for sn-glycerol-3-phosphate acyltransferase from Phaseolus vulgaris."
Fritz M., Heinz E., Wolter F.P.
Plant Physiol. 107:1039-1040(1995) [PubMed: 7716242] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Annabel.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79722 mRNA. Translation: CAA56159.1.
PIRT11819.

3D structure databases

SMRQ43822. Positions 97-460.
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.3.1.15. 8.

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_PHAVU
AccessionPrimary (citable) accession number: Q43822
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: February 9, 2010
This is version 57 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