DB code: D00874

CATH domain	1.10.1200.50 : Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein; Chain A
CATH domain	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

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.
MAP00561	Glycerolipid metabolism
MAP00564	Glycerophospholipid 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 15978	15346 15346
PubChem			439162 439162	6816 87642 6816 87642

1iuqA01	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1k30A01	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1iuqA02	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1k30A02	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
1k30A01
1iuqA02	HIS 139;ASP 144
1k30A02	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.

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