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Reviewed, UniProtKB/Swiss-Prot Q9LLY4 (LPAT1_BRANA)

Last modified June 16, 2009. Version 31. 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:
    1-acyl-sn-glycerol-3-phosphate acyltransferase 1, chloroplastic
    EC=2.3.1.51
Gene names
Name: LPAT1
Synonyms: ACT2, BAT2
OrganismBrassica napus (Rape)
Taxonomic identifier3708 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeBrassica

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position. Has preference for C-16-CoA substrates compared to C-18-CoA substrates.

Catalytic activity

Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate. Ref.1

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.

Subcellular location

Plastidchloroplast membrane; Multi-pass membrane protein. Ref.1

Tissue specificity

Ubiquitously expressed. Ref.1

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 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentChloroplast
Membrane
Plastid
   DomainTransit peptide
Transmembrane
   Molecular functionAcyltransferase
Transferase
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function1-acylglycerol-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 – 8787Chloroplast Potential
Chain88 – 3442571-acyl-sn-glycerol-3-phosphate acyltransferase 1, chloroplastic
PRO_0000024702

Regions

Transmembrane113 – 13321 Potential
Transmembrane210 – 23021 Potential
Motif188 – 1936HXXXXD motif

Sequences

Sequence LengthMass (Da)Tools
Q9LLY4-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: B666D9C8AA09AB33

FASTA34437,998
        10         20         30         40         50         60 
MDVASARGVS SHPPYYSKPI CSSQSSLIRI PISKGCCFAR SSNLITSLHA ASRGVTRRTS 

        70         80         90        100        110        120 
GVQWCYRSIR FDPFKVNDKN SRTVTVRSDL SGAATPESTY PEPEIKLSSR LRGICFCLVA 

       130        140        150        160        170        180 
GISAIVLIVL MIIGHPFVLL FDRYRRKFHH FIAKLWASIS IYPFYKTDIQ GLENLPSSDT 

       190        200        210        220        230        240 
PCVYVSNHQS FLDIYTLLSL GQSYKFISKT GIFVIPVIGW AMSMMGVVPL KRMDPRSQVD 

       250        260        270        280        290        300 
CLKRCMELVK KGASVFFFPE GTRSKDGRLG PFKKGAFTIA AKTGVPVVPI TLMGTGKIMP 

       310        320        330        340 
TGSEGILNHG DVRVIIHKPI YGSKADVLCE EARNKIAESM NLLS 

« Hide

References

[1]"A plastidial lysophosphatidic acid acyltransferase from oilseed rape."
Bourgis F., Kader J.-C., Barret P., Renard M., Robinson D., Robinson C., Delseny M., Roscoe T.J.
Plant Physiol. 120:913-922(1999) [PubMed: 10398728] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases

AF111161 mRNA. Translation: AAF73736.1.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA2.3.1.51. 393.

Family and domain databases

InterProIPR002123. Acyltransferase.
IPR004552. AGP_acyltrans.
[Graphical view]
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsTIGR00530. AGP_acyltrn. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLPAT1_BRANA
AccessionPrimary (citable) accession number: Q9LLY4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 31 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