DB code: D00874

CATH domain 1.10.1200.50 : Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein; Chain A
3.40.1130.10 : Glycerol-3-phosphate (1)-acyltransferase Catalytic domain
E.C. 2.3.1.15
CSA 1k30
M-CSA 1k30
MACiE

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P10349 Glycerol-3-phosphate acyltransferase, chloroplastic
GPAT
EC 2.3.1.15
PF01553 (Acyltransferase)
[Graphical View]

KEGG enzyme name
glycerol-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

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P10349 PLSB_CUCMO Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate. Plastid, chloroplast stroma.

KEGG Pathways
Map code Pathways E.C.
MAP00564 Glycerophospholipid metabolism
MAP00561 Glycerolipid metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00040 C00173 C00093 C00010 C00229 C00681 I00150
E.C.
Compound Acyl-CoA Acyl-[acyl-carrier protein] sn-Glycerol 3-phosphate CoA Acyl-carrier protein (EzCatDB U00001) 1-Acyl-sn-glycerol 3-phosphate [CoA/ACP]-tetrahedral-acyl-sn-glycerol 3-phosphate
Type amine group,carbohydrate,nucleotide ,peptide/protein,sulfide group carbohydrate,peptide/protein,phosphate group/phosphate ion,sulfide group carbohydrate,phosphate group/phosphate ion amine group,carbohydrate,nucleotide ,peptide/protein,sulfhydryl group carbohydrate,peptide/protein,phosphate group/phosphate ion,sulfhydryl group carbohydrate,lipid,phosphate group/phosphate ion
ChEBI 15978
15346
PubChem 439162
6816
87642
1iuqA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k30A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1iuqA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k30A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [2], [3]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1iuqA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k30A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1iuqA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 139;ASP 144
1k30A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 139;ASP 144

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
p.1429
[2]
p.349-351
[3]
p.19-20

References
[1]
Resource
Comments
Medline ID
PubMed ID 9515909
Journal J Bacteriol
Year 1998
Volume 180
Pages 1425-30
Authors Heath RJ, Rock CO
Title A conserved histidine is essential for glycerolipid acyltransferase catalysis.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 11377195
Journal Structure
Year 2001
Volume 9
Pages 347-53
Authors Turnbull AP, Rafferty JB, Sedelnikova SE, Slabas AR, Schierer TP, Kroon JT, Simon JW, Fawcett T, Nishida I, Murata N, Rice DW
Title Analysis of the structure, substrate specificity, and mechanism of squash glycerol-3-phosphate (1)-acyltransferase.
Related PDB 1k30
Related UniProtKB P10349
[3]
Resource
Comments
Medline ID
PubMed ID 14684887
Journal Acta Crystallogr D Biol Crystallogr
Year 2004
Volume 60
Pages 13-21
Authors Tamada T, Feese MD, Ferri SR, Kato Y, Yajima R, Toguri T, Kuroki R
Title Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea.
Related PDB 1iuq
Related UniProtKB P10349
[4]
Resource
Comments
Medline ID
PubMed ID 19903225
Journal J Integr Plant Biol
Year 2009
Volume 51
Pages 1040-9
Authors Zhu SQ, Zhao H, Zhou R, Ji BH, Dan XY
Title Substrate selectivity of glycerol-3-phosphate acyl transferase in rice.
Related PDB
Related UniProtKB

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.

Created Updated
2012-10-10 2012-10-11