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Q59188 (PLSC_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. 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:
1-acyl-sn-glycerol-3-phosphate acyltransferase

Short name=1-AGP acyltransferase
Short name=1-AGPAT
EC=2.3.1.51
Alternative name(s):
Lysophosphatidic acid acyltransferase
Short name=LPAAT
Gene names
Name:plsC
Ordered Locus Names:BB_0037
OrganismBorrelia burgdorferi (Lyme disease spirochete)
Taxonomic identifier139 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position.

Catalytic activity

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

Pathway

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

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
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmembrane

Inferred from electronic annotation. Source: InterPro

   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

Chain1 – 2502501-acyl-sn-glycerol-3-phosphate acyltransferase
PRO_0000208167

Regions

Motif88 – 936HXXXXD motif

Sequences

Sequence LengthMass (Da)Tools
Q59188 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: A730BED7058AD999

FASTA25028,581
        10         20         30         40         50         60 
MIIVFMKILR SIITYFNVLL FFLILIFFLF PFYLVCKIFL IERYVVRLSF IMMRACIKIS 

        70         80         90        100        110        120 
LWLAGIKIIV TGSENIPKKS NVIIMGNHIA AMDPLIFIYT FACPFVILAK HSLLRIPFVN 

       130        140        150        160        170        180 
IVLIVMGVIF VNRRSIRSAA AAEVKAIKVM REGRSIGIFP EGTRNRGGDT RVFKKGSIKM 

       190        200        210        220        230        240 
ALKTGTSILP VTLYNTNNFF IKNIIFNSGL SVYIHVHPLI DVLKLSEYEK ENLTSIIRDQ 

       250 
IVKKLETIKI 

« Hide

References

« Hide 'large scale' references
[1]"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi."
Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. expand/collapse author list , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C.
Nature 390:580-586(1997) [PubMed: 9403685] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[2]"Conservation of gene arrangement and an unusual organization of rRNA genes in the linear chromosomes of the Lyme disease spirochaetes Borrelia burgdorferi, B. garinii and B. afzelii."
Ojaimi C., Davidson B.E., Saint-Girons I., Old I.G.
Microbiology 140:2931-2940(1994) [PubMed: 7812434] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-250.
Strain: 212.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000783 Genomic DNA. Translation: AAC66417.1.
L32861 Genomic DNA. Translation: AAC41407.1.
PIRE70104.
RefSeqNP_212171.1. NC_001318.1.

3D structure databases

ProteinModelPortalQ59188.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBORT00000008608; EBBORP00000007938; EBBORG00000008607.
GeneID1194873.
GenomeReviewsGene locus BB_0037 in contig AE000783_GR.
KEGGbbu:BB0037.
NMPDRfig|224326.1.peg.421.
PATRIC20556679. VBIBorBur75917_0436.
TIGRBB_0037.

Phylogenomic databases

GeneTreeEBGT00050000006883.
HOGENOMHBG354607.
OMALERYVIR.
PhylomeDBQ59188.
ProtClustDBCLSK507308.

Enzyme and pathway databases

BioCycBBUR224326:BB_0037-MONOMER.

Family and domain databases

InterProIPR002123. Acyltransferase.
IPR004552. AGP_acyltrans.
[Graphical view]
KOK00655.
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsTIGR00530. AGP_acyltrn. 1 hit.
ProtoNetSearch...

Entry information

Entry namePLSC_BORBU
AccessionPrimary (citable) accession number: Q59188
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: January 25, 2012
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families