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Q089E1 (PLSB_SHEFN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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

Short name=GPAT
EC=2.3.1.15
Gene names
Name:plsB
Ordered Locus Names:Sfri_0261
OrganismShewanella frigidimarina (strain NCIMB 400) [Complete proteome] [HAMAP]
Taxonomic identifier318167 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length807 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate. HAMAP MF_00393

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. HAMAP MF_00393

Subcellular location

Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity HAMAP MF_00393.

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. HAMAP MF_00393

Sequence similarities

Belongs to the GPAT/DAPAT family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentCell inner membrane
Cell membrane
Membrane
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

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

Chain1 – 807807Glycerol-3-phosphate acyltransferase HAMAP MF_00393
PRO_1000049457

Regions

Motif308 – 3136HXXXXD motif HAMAP MF_00393

Sequences

Sequence LengthMass (Da)Tools
Q089E1 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: F3AAA95E1FBB6CED

FASTA80791,990
        10         20         30         40         50         60 
MSKPDSIFLR ALRWIQKWMV QTIVVPHDPF DDLNIDPTKP LVYLMKTESI SDIAALSEIT 

        70         80         90        100        110        120 
EGFGLPSPYE PLQLDGLTVP RVVCLEGRKP LFGKRESGDK FLNYFTSLLS LHSESPELDI 

       130        140        150        160        170        180 
QLVPVCLYWG RTPGKEEDSM KAAVFERENP TWLRKWLMIL FLGRHNFVQF SNALSLRHMA 

       190        200        210        220        230        240 
DEHGTDKRIA HKLTRVARVH FRRQRKVMTG PQLPNRQALF ASLLKSESIK KAIEEESANK 

       250        260        270        280        290        300 
KVTVEKARET AIEYLDEIAA DYSDSLVRIA ERFLTWLWNK LYSGINIKGA EQVRQLHHDG 

       310        320        330        340        350        360 
HEIVYVPCHR SHMDYLLLSY ILYYQGMVPP HIAAGINLNF WPAGPMFRRG GAFFIRRSFN 

       370        380        390        400        410        420 
GNKLYTAVFR EYLDQLFAKG YAVEYFTEGG RSRTGRLLAP KTGMLAMTIN SVLRGIERPV 

       430        440        450        460        470        480 
TLVPVYLGYD HVMEVATYHK ELSGKKKKKE SVWQVFGAIR KLGNFGQGYV NFGEPINLQQ 

       490        500        510        520        530        540 
FLNQQAPEWR DELAKDPDQK PSWFTPSVNL LANRVMTNIN GAAAASSVTL TSLVLLASEQ 

       550        560        570        580        590        600 
NALERSQLER QLDLYLALLK TVPYTEYASV AEGNGKSIVD HCLSLNKFVS TKDLIGEIIS 

       610        620        630        640        650        660 
VDEKIAITMS YYRNNIIHLM ALPSLIASCL VHYDVCDRQR IHAIVMDFYP LLKAELFMSI 

       670        680        690        700        710        720 
DDVPKHVDCI LDFMVEQGLL TGSDQFEITP RHITQVLLLA ETISETLQRY AIIFNLLAIK 

       730        740        750        760        770        780 
PDLERSELER DSHLLAQRLG ALHGITAPEF YDKKLYNTLS VKLKELGYLC SDEHRAEVIR 

       790        800 
IRDNANKLLS SLVRQTIVDS VEAEHGQ 

« Hide

References

[1]"Complete sequence of Shewanella frigidimarina NCIMB 400."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H., Newman D., Tiedje J.M. expand/collapse author list , Zhou J., Romine M.F., Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCIMB 400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000447 Genomic DNA. Translation: ABI70124.1.
RefSeqYP_748962.1. NC_008345.1.

3D structure databases

ProteinModelPortalQ089E1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ089E1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4277032.
GenomeReviewsGene locus Sfri_0261 in contig CP000447_GR.
KEGGsfr:Sfri_0261.
NMPDRfig|318167.10.peg.250.
PATRIC23494285. VBISheFri14343_0273.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2937.
HOGENOMHBG296590.
OMAWNKLYQG.
ProtClustDBPRK04974.

Family and domain databases

HAMAPMF_00393. Glyc3P_acyltrans.
[Tree]
InterProIPR002123. Acyltransferase.
IPR022284. G3P_O-AcylTrfase.
[Graphical view]
KOK00631.
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFPIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsTIGR03703. PlsB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePLSB_SHEFN
AccessionPrimary (citable) accession number: Q089E1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 31, 2006
Last modified: January 25, 2012
This is version 37 of the entry and version 1 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