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Q5QUP4 (Q5QUP4_IDILO) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glycerol-3-phosphate acyltransferase HAMAP MF_00393

Short name=GPAT HAMAP MF_00393
EC=2.3.1.15 HAMAP MF_00393
Gene names
Name:plsB HAMAP MF_00393 EMBL AAV81106.1
Ordered Locus Names:IL0263
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length840 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 SAAS SAAS002123

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. HAMAP MF_00393 SAAS SAAS002123

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. HAMAP MF_00393

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Motif302 – 3076HXXXXD motif By similarity HAMAP MF_00393

Sequences

Sequence LengthMass (Da)Tools
Q5QUP4 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 249FBBF5B7B098B5

FASTA84095,202
        10         20         30         40         50         60 
MKGISRFFPI FKYPLRWLTR FQEIWDGTEE EHSATVGKPI VYVMRSTSKA DLSILQRAAH 

        70         80         90        100        110        120 
KRGLPDPVDP LVVNGKTYNR IMYLEELANE VSDQTVSEFH QLLTLHKDQP ELDVQLIPAG 

       130        140        150        160        170        180 
VFWGRQAGEE AHAGNTMTGD LDNPGHWRKF WLVIFSGRQV LLRFSRSVSL GTMARDHGTD 

       190        200        210        220        230        240 
MRIAHKLARV ARVHFVRMRH AVAGPKLSQR KELMSALINT PALKKAVSDE ARGKKISEEA 

       250        260        270        280        290        300 
ARKRALSYID EIAANYNSTL IRVLDRFMTW MWNRIYNGIH VKGGDTIRRL AQQGHEVIYV 

       310        320        330        340        350        360 
PCHRSHMDYL LLSYVIYKEG LVPPHIAAGV NLNFFPVGGI FRRGGAFFIR RSFRGNKLYS 

       370        380        390        400        410        420 
AVFREYLCWL FQKGYPVEYF SEGGRSRTGR LLPPKTGMLA MTVQGMLRDQ QRPVSLVPVY 

       430        440        450        460        470        480 
LGYEHIMEVA TYLKELKGKD KEKESVFQIL KTVAKLRNFG QGFVTFGQPI NLKHHLDKVA 

       490        500        510        520        530        540 
PNWHESVTRG AQEPERPGWL NPVVGGLAEQ VMQGINDSAA ANSVNLTALA LLSSEHHALM 

       550        560        570        580        590        600 
KEELLAQLEV YLGVLREVPY SNMMSVPEET PEELWQQALR TDKFTVDSDT MGEVVSLERM 

       610        620        630        640        650        660 
TAIAMTYYRN NILHLMVVPG IVASIIMAKK KVSVAEIGAR TQAIYPSLKA ELYLSHNVED 

       670        680        690        700        710        720 
LPLWTEALAE ELARQKLITL EDGVCTIAQR ESAQWYRLRL LANSASETLQ RYCIVLELLQ 

       730        740        750        760        770        780 
QAQPIMRADL EKQSITLAER LSSIHGIDAP EFYDKKVMST LIASLKQQGL VEINDDGQQI 

       790        800        810        820        830        840 
AAEPVGELSD QVDELIDGPV LQTIRQSVEQ FVQQLKEQAE HEQKEAPKEE QKPTESNQNQ 

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References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV81106.1.
RefSeqYP_154655.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QUP4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3172680.
GenomeReviewsGene locus IL0263 in contig AE017340_GR.
KEGGilo:IL0263.
NMPDRfig|283942.3.peg.254.
PATRIC22138535. VBIIdiLoi21852_0264.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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 nameQ5QUP4_IDILO
AccessionPrimary (citable) accession number: Q5QUP4
Entry history
Integrated into UniProtKB/TrEMBL: January 4, 2005
Last sequence update: January 4, 2005
Last modified: December 14, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)