EzCatDB: D00874
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DB codeD00874
CATH domainDomain 11.10.1200.50 : Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein; Chain A
Domain 23.40.1130.10 : Glycerol-3-phosphate (1)-acyltransferaseCatalytic domain
E.C.2.3.1.15
CSA1k30


Enzyme Name
UniProtKBKEGG

P10349
Protein nameGlycerol-3-phosphate acyltransferase, chloroplasticglycerol-3-phosphate 1-O-acyltransferase
alpha-glycerophosphate acyltransferase
3-glycerophosphate acyltransferase
ACP:sn-glycerol-3-phosphate acyltransferase
glycerol 3-phosphate acyltransferase
glycerol phosphate acyltransferase
glycerol phosphate transacylase
glycerophosphate acyltransferase
glycerophosphate transacylase
sn-glycerol 3-phosphate acyltransferase
sn-glycerol-3-phosphate acyltransferase
glycerol-3-phosphate O-acyltransferase
SynonymsGPAT
EC 2.3.1.15
PfamPF01553 (Acyltransferase)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00561Glycerolipid metabolism
MAP00564Glycerophospholipid metabolism

UniProtKB:Accession NumberP10349
Entry namePLSB_CUCMO
ActivityAcyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.
Subunit
Subcellular locationPlastid, chloroplast stroma.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00040C00173C00093C00010C00229C00681I00150
CompoundAcyl-CoAAcyl-[acyl-carrier protein]sn-Glycerol 3-phosphateCoAAcyl-carrier protein (EzCatDB U00001)1-Acyl-sn-glycerol 3-phosphate[CoA/ACP]-tetrahedral-acyl-sn-glycerol 3-phosphate
Typeamine group,carbohydrate,nucleotide,peptide/protein,sulfide groupcarbohydrate,peptide/protein,phosphate group/phosphate ion,sulfide groupcarbohydrate,phosphate group/phosphate ionamine group,carbohydrate,nucleotide,peptide/protein,sulfhydryl groupcarbohydrate,peptide/protein,phosphate group/phosphate ion,sulfhydryl groupcarbohydrate,lipid,phosphate group/phosphate ion
ChEBI

15978
15346



PubChem

439162
87642
6816



               
1iuqA01UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1k30A01UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1iuqA02UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1k30A02UnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [2], [3]
pdbCatalytic residues
         
1iuqA01 
1k30A01 
1iuqA02HIS 139;ASP 144
1k30A02HIS 139;ASP 144

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.1429
[2]p.349-351
[3]p.19-20

references
[1]
PubMed ID9515909
JournalJ Bacteriol
Year1998
Volume180
Pages1425-30
AuthorsHeath RJ, Rock CO
TitleA conserved histidine is essential for glycerolipid acyltransferase catalysis.
[2]
PubMed ID11377195
JournalStructure
Year2001
Volume9
Pages347-53
AuthorsTurnbull AP, Rafferty JB, Sedelnikova SE, Slabas AR, Schierer TP, Kroon JT, Simon JW, Fawcett T, Nishida I, Murata N, Rice DW
TitleAnalysis of the structure, substrate specificity, and mechanism of squash glycerol-3-phosphate (1)-acyltransferase.
Related PDB1k30
Related UniProtKBP10349
[3]
PubMed ID14684887
JournalActa Crystallogr D Biol Crystallogr
Year2004
Volume60
Pages13-21
AuthorsTamada T, Feese MD, Ferri SR, Kato Y, Yajima R, Toguri T, Kuroki R
TitleSubstrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea.
Related PDB1iuq
Related UniProtKBP10349
[4]
PubMed ID19903225
JournalJ Integr Plant Biol
Year2009
Volume51
Pages1040-9
AuthorsZhu SQ, Zhao H, Zhou R, Ji BH, Dan XY
TitleSubstrate selectivity of glycerol-3-phosphate acyl transferase in rice.

comments
According to the literature [2] and [3], accyl-carrier protein (C00229) and its acylated protein (C00173) are included as product and substrate, respectively, in this entry.
According to the literature[2] adn [3], the charge relay system, composed of His139 and Asp144, can contribute to the transfer reaction of the acyl chain from either CoA or Acyl-carrier protein (ACP) to the sn-1 hydroxyl group of Glycerol 3-phosphate (G3P), in analogy with those reactions by serine proteases.
Here, Asp144 may modulate the activity of His139, which acts as a general base to deprotonate the acyl acceptor group (or the hydroxyl group) of G3P. The deprotonated hydroxyl group can make a nucleophilic attack on the acyl group, forming a tetrahedral intermediate (I00150).
However, it is not clear how the oxyanion of the intermediate can be stabilized.

createdupdated
2012-10-102012-10-11


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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