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Protein

Glycerol-3-phosphate acyltransferase

Gene

plsB

Organism
Shewanella sediminis (strain HAW-EB3)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.UniRule annotation

Pathwayi: CDP-diacylglycerol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glycerol-3-phosphate acyltransferase (plsB)
  2. no protein annotated in this organism
  3. Phosphatidate cytidylyltransferase (Ssed_3156)
This subpathway is part of the pathway CDP-diacylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate, the pathway CDP-diacylglycerol biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BioCyciSSED425104:GH7Q-204-MONOMER.
UniPathwayiUPA00557; UER00612.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate acyltransferaseUniRule annotation (EC:2.3.1.15UniRule annotation)
Short name:
GPATUniRule annotation
Gene namesi
Name:plsBUniRule annotation
Ordered Locus Names:Ssed_0201
OrganismiShewanella sediminis (strain HAW-EB3)
Taxonomic identifieri425104 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000002015 Componenti: Chromosome

Subcellular locationi

  • Cell inner membrane UniRule annotation; Peripheral membrane protein UniRule annotation; Cytoplasmic side UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 807807Glycerol-3-phosphate acyltransferasePRO_1000080294Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi425104.Ssed_0201.

Structurei

3D structure databases

ProteinModelPortaliA8FPP1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi308 – 3136HXXXXD motif

Domaini

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.UniRule annotation

Sequence similaritiesi

Belongs to the GPAT/DAPAT family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105E55. Bacteria.
COG2937. LUCA.
HOGENOMiHOG000218231.
KOiK00631.
OMAiEVIYVPC.
OrthoDBiPOG091H06BX.

Family and domain databases

HAMAPiMF_00393. Glyc3P_acyltrans. 1 hit.
InterProiIPR022284. GPAT/DHAPAT.
IPR028354. GPAT_PlsB.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 2 hits.
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFiPIRSF500064. GPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03703. plsB. 1 hit.

Sequencei

Sequence statusi: Complete.

A8FPP1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKQDSLWFK SLRWLQNKLV HTIVVPHEPF KDLNLDPDKP LAYVMKTESV
60 70 80 90 100
SDIAALSEIT ADLGLPSPYQ PLEVGGESAP RVVCLEGAKP LMGKRESNHF
110 120 130 140 150
FLNSFMSLLK IHKERPELDI QLVPVSLYWG RTPGKEDDTM KAAVLERENP
160 170 180 190 200
TWLRKCLMIL FLGRHNFVQF SSAVSLRYMA DEHGTDKRIA QKLARVARVH
210 220 230 240 250
FSRQRKVMTG PVLPKRQALF HALINSETLK KAIQEEAASK KITEVEARAK
260 270 280 290 300
AMEYLDEIAA DYSDSLVRIA ERFLTWLWNK LYKGINIKGA EEVRRLHHDG
310 320 330 340 350
HEIIYVPCHR SHMDYLLLSY ILYYQGMVPP HIAAGINLNF WPAGPMFRRG
360 370 380 390 400
GAFFIRRSFR GNKLYTTVFR EYLDQLFTKG YSVEYFTEGG RSRTGRLLAP
410 420 430 440 450
KTGMLAMTLN SVLRGMKRPV TLVPVYLGYD HVMEVATYHK ELSGKKKKKE
460 470 480 490 500
SVWQVFGALR KLGNFGQGYV NFGKPITLHS FLNEQKPDWK EEIAKEPEQR
510 520 530 540 550
PKWLTPMVNT LANQVMTNIN DAAAVSSVTL TSLVLLASEQ NALERSQLEK
560 570 580 590 600
QLDLYLKLLK DLPYTSYTSV VEGDGKSLVQ QGLELKKIKL DSDPLGDIIS
610 620 630 640 650
IDESIAVAMT YYRNNIIHLM VIPSLVASCL TQHEHISRDE IIDIIKDFYP
660 670 680 690 700
LLQAELFMGV EDTDKLVGQI LDLFIAQGLV TEDDGFSIIE TEVNQLLLLA
710 720 730 740 750
GTVGETLQRY AIIFNLLAVC PKMERSDLER ESHKLAQRLG ALHGITAPEF
760 770 780 790 800
YDKKLYGALS VKLKELGYLS DNGNKVDVQR IRERANGLLR SSVRQTIVDS

VTAEHKD
Length:807
Mass (Da):91,667
Last modified:November 13, 2007 - v1
Checksum:i6DB8A335BE6119B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000821 Genomic DNA. Translation: ABV34814.1.
RefSeqiWP_012004340.1. NC_009831.1.

Genome annotation databases

EnsemblBacteriaiABV34814; ABV34814; Ssed_0201.
KEGGisse:Ssed_0201.
PATRICi23557552. VBISheSed62411_0211.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000821 Genomic DNA. Translation: ABV34814.1.
RefSeqiWP_012004340.1. NC_009831.1.

3D structure databases

ProteinModelPortaliA8FPP1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi425104.Ssed_0201.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV34814; ABV34814; Ssed_0201.
KEGGisse:Ssed_0201.
PATRICi23557552. VBISheSed62411_0211.

Phylogenomic databases

eggNOGiENOG4105E55. Bacteria.
COG2937. LUCA.
HOGENOMiHOG000218231.
KOiK00631.
OMAiEVIYVPC.
OrthoDBiPOG091H06BX.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00612.
BioCyciSSED425104:GH7Q-204-MONOMER.

Family and domain databases

HAMAPiMF_00393. Glyc3P_acyltrans. 1 hit.
InterProiIPR022284. GPAT/DHAPAT.
IPR028354. GPAT_PlsB.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 2 hits.
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFiPIRSF500064. GPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03703. plsB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPLSB_SHESH
AccessioniPrimary (citable) accession number: A8FPP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: September 7, 2016
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.