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Protein

Glycerol-3-phosphate acyltransferase

Gene

plsB

Organism
Shewanella baltica (strain OS185)
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. no protein annotated in this organism
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

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:Shew185_4177
OrganismiShewanella baltica (strain OS185)
Taxonomic identifieri402882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

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)DescriptionActionsGraphical viewLength
ChainiPRO_10000494551 – 807Glycerol-3-phosphate acyltransferaseAdd BLAST807

Structurei

3D structure databases

ProteinModelPortaliA6WU04.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi308 – 313HXXXXD motif6

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

HOGENOMiHOG000218231.
KOiK00631.
OMAiEVIYVPC.

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.

A6WU04-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKHDSLWLK SLRWIQKHLV HTIVVPQDPF ADLNLDASRP LAYVMKTESL
60 70 80 90 100
SDIAALSEIT AKLGLPSPYE PLVANGVIAP RVVCLQGRKP LFGERAGNEP
110 120 130 140 150
FLECFMRLLA VHKERPELDI QLVPVSLYWG RTPGKEDDTM KAAVFERENP
160 170 180 190 200
TWLRKCLMIL FLGRHNFVQF SNAVSLRYMA DEHGTDMGIA HKLARVARVH
210 220 230 240 250
FRRQRKVMTG PVLPNRQALF HSLLKSESLR KAIQEEAANK KISETQARET
260 270 280 290 300
AIEYLDEIAA DYSDSLVRIA ERFLTWLWNK LYSGINIKGA EQVRQLHHDG
310 320 330 340 350
HEIVYVPCHR SHMDYLLLSY ILYYQGMVPP HIAAGINLNF WPAGPMFRRG
360 370 380 390 400
GAFFIRRSFN GNKLYTAVFR EYLDQLFAKG YSVEYFSEGG RSRTGRLLAP
410 420 430 440 450
KTGMIAMTMN SVLRGIERPV TLVPVYLGYD HVMEVATYHK ELSGKKKKKE
460 470 480 490 500
SVWQVFGAIR KLGNFGQGYV NFGEPITLQN FLNERAPNWR TELADDPEQK
510 520 530 540 550
PSWLTPAVNV LANRVMTNIN DAAAASSVTL TSLVLLATDQ NALERSLLER
560 570 580 590 600
QLDLYLTLLK KVPYTTYTSV AEGDGKHLVQ QGLELNKFVV CADPLGEIVS
610 620 630 640 650
IEASQAVSMT YYRNNIIHLF IVPSLIASCL THNEQIPRQQ VVSIVADFYP
660 670 680 690 700
LLKAELFMGI KDVPAYVNQV LDFFIEQGLV VETDTLTVVP EHTSQLLLLA
710 720 730 740 750
SSVSETLQRY AIIFNLLANR PKMERSELES ESHLLAQRLG ALHGITAPEF
760 770 780 790 800
YDKKLYGTLS VKLKELGYLA DNQDKSNINR IRDQANSLLR PSVKQTIVAS

VTAEHTV
Length:807
Mass (Da):91,246
Last modified:August 21, 2007 - v1
Checksum:iEC411E4A16AE2C73
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000753 Genomic DNA. Translation: ABS10293.1.
RefSeqiWP_006079610.1. NC_009665.1.

Genome annotation databases

EnsemblBacteriaiABS10293; ABS10293; Shew185_4177.
GeneIDi11774285.
KEGGisbm:Shew185_4177.
PATRICi23465465. VBISheBal127872_4464.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000753 Genomic DNA. Translation: ABS10293.1.
RefSeqiWP_006079610.1. NC_009665.1.

3D structure databases

ProteinModelPortaliA6WU04.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS10293; ABS10293; Shew185_4177.
GeneIDi11774285.
KEGGisbm:Shew185_4177.
PATRICi23465465. VBISheBal127872_4464.

Phylogenomic databases

HOGENOMiHOG000218231.
KOiK00631.
OMAiEVIYVPC.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00612.

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_SHEB8
AccessioniPrimary (citable) accession number: A6WU04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: November 2, 2016
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.