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Reviewed, UniProtKB/Swiss-Prot Q0I2G8 (PLSB_HAES1)

Last modified January 19, 2010. Version 28. 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
      Short name=GPAT
    EC=2.3.1.15
Gene names
Name: plsB
Ordered Locus Names: HS_0385
OrganismHaemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

Protein attributes

Sequence length811 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 membrane; Peripheral membrane protein 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 membrane
Membrane
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentextrinsic to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: HAMAP

   Molecular functionglycerol-3-phosphate O-acyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 811811Glycerol-3-phosphate acyltransferase HAMAP MF_00393
PRO_1000049436

Regions

Motif305 – 3106HXXXXD motif HAMAP MF_00393

Sequences

Sequence LengthMass (Da)Tools
Q0I2G8-1 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 61444F0420B80C71

FASTA81192,687
        10         20         30         40         50         60 
MSSILNFYRN LLSVPLSFLV KNNPIPQQPI EELSLDISQP IIYLLPYTSQ TDLIIIRKNC 

        70         80         90        100        110        120 
LSVGLPDPLE ENELGGQCLP RYVFLDEGRR FFKSKGAKSA TIQIVEKYLE LHRSLPDLNV 

       130        140        150        160        170        180 
QLVPVSVLWG RSPGHEKQVG LPKLRLLNSI QKTAVAIWFG RDTFVRFSQA VSLRYMADEY 

       190        200        210        220        230        240 
GTDASIALKL ARVAKIHFAK QRMSATGPRL PNRQAMFNKL LQSPAILNAI ADEAKSKRIS 

       250        260        270        280        290        300 
KEKARKEAYK ILDEIAANVN YEGLRVADRF LGWLWNKLYQ GIDVQNAERV RKLALEGHEI 

       310        320        330        340        350        360 
VYIPCHRSHI DYLLLSYVLY HQGLVPPHIA AGINLNFWPV GMMFRRGGAF FIRRTFKGNR 

       370        380        390        400        410        420 
LYSTIFREYL AELFHRGYSV EFFIEGGRSR TGRLLAPKTG MMSMTVQALQ QNQIRPISVV 

       430        440        450        460        470        480 
PVYVGYEHVL EVDTYAKELR GAAKEKENAG LVLRVIRKLR NLGQGYVNFA EPITLSNYLN 

       490        500        510        520        530        540 
QHFPEWKDSQ LEEHSQWFNP AVNAISNQVM ININKAAAIN AMNLTGTALL SSRQRALSRE 

       550        560        570        580        590        600 
QLLEQLKSYQ RFLQHAPYSN DIIVPTDTPE EILTHVLNLE RVGLIVEKDN FGEMLRLERS 

       610        620        630        640        650        660 
AAVLMTYYRN NIQHVFVLPS LIASIIFHHG AIQKELVSNA ARKIYPFLKE ELFLHFSQDE 

       670        680        690        700        710        720 
LDEYVEKIIE EFTRQKLILC AENLLSINKE RVRVLQLWMA GVREILQRYY ITVSILQDTP 

       730        740        750        760        770        780 
NIAKATLEKE SQSIAQRLSV LHGINAPEFF DKAVFSAFIG SLRSNGYFDK NGVAITEKLN 

       790        800        810 
DISDILDRII STEVQLTIKS AVGKHEEVQE Y 

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References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed: 17172329] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000436 Genomic DNA. Translation: ABI24663.1.
RefSeqYP_718595.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ0I2G8.

Genome annotation databases

GeneID4239861.
GenomeReviewsGene locus HS_0385 in contig CP000436_GR.
KEGGhso:HS_0385.
NMPDRfig|205914.1.peg.94.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2937.
HOGENOMHBG296590.
OMAWNKLYQG.

Enzyme and pathway databases

BioCycHSOM205914:HS_0385-MONOMER.

Family and domain databases

HAMAPMF_00393. Glyc3P_acyltrans.
[Tree]
InterProIPR002123. Acyltransferase.
[Graphical view]
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLSB_HAES1
AccessionPrimary (citable) accession number: Q0I2G8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: January 19, 2010
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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