P10349 (PLSB_CUCMO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Glycerol-3-phosphate acyltransferase, chloroplastic Short name=GPAT EC=2.3.1.15
Organism	Cucurbita moschata (Winter crookneck squash) (Cucurbita pepo var. moschata)
Taxonomic identifier	3662 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Cucurbitales › Cucurbitaceae › Cucurbiteae › Cucurbita

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate. The enzyme from chilling-resistant plants discriminates against non-fluid palmitic acid and selects oleic acid whereas the enzyme from sensitive plants accepts both fatty acids. Squash is chilling-sensitive.
Catalytic activity	Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.
Pathway	Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
Subcellular location	Plastid › chloroplast stroma.
Domain	The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence similarities	Belongs to the GPAT/DAPAT family.
Caution	May represent a 5'-truncated sequence in which part of the leader sequence is missing.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	CDP-diacylglycerol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	chloroplast stroma Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glycerol-3-phosphate O-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 28

28

Chloroplast

Chain

29 – 396

368

Glycerol-3-phosphate acyltransferase, chloroplastic

PRO_0000024696

Regions

Motif

167 – 172

6

HXXXXD motif

Secondary structure

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396

Helix Strand Turn

Details...

Helix

35 – 38

4

Helix

42 – 54

13

Helix

60 – 79

20

Helix

85 – 105

21

Beta strand

112 – 114

3

Beta strand

119 – 121

3

Helix

123 – 131

9

Helix

132 – 134

3

Helix

137 – 139

3

Beta strand

141 – 143

3

Helix

145 – 156

12

Beta strand

160 – 165

6

Helix

172 – 180

9

Turn

181 – 183

3

Helix

185 – 190

6

Beta strand

192 – 195

4

Helix

198 – 201

4

Turn

203 – 205

3

Helix

206 – 210

5

Beta strand

212 – 216

5

Helix

220 – 222

3

Helix

227 – 229

3

Helix

230 – 250

21

Beta strand

254 – 257

4

Turn

268 – 270

3

Helix

280 – 291

12

Beta strand

293 – 295

3

Beta strand

297 – 305

9

Helix

307 – 309

3

Helix

315 – 319

5

Beta strand

332 – 335

4

Helix

341 – 346

6

Beta strand

348 – 350

3

Helix

351 – 376

26

Turn

377 – 379

3

Helix

382 – 385

4

Sequences

	Sequence		Length	Mass (Da)
	P10349 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: CB96E8C057B88112	FASTA	396	43,839
	10 20 30 40 50 60 MAELIQDKES AQSAATAAAA SSGYERRNEP AHSRKFLDVR SEEELLSCIK KETEAGKLPP 70 80 90 100 110 120 NVAAGMEELY QNYRNAVIES GNPKADEIVL SNMTVALDRI LLDVEDPFVF SSHHKAIREP 130 140 150 160 170 180 FDYYIFGQNY IRPLIDFGNS FVGNLSLFKD IEEKLQQGHN VVLISNHQTE ADPAIISLLL 190 200 210 220 230 240 EKTNPYIAEN TIFVAGDRVL ADPLCKPFSI GRNLICVYSK KHMFDIPELT ETKRKANTRS 250 260 270 280 290 300 LKEMALLLRG GSQLIWIAPS GGRDRPDPST GEWYPAPFDA SSVDNMRRLI QHSDVPGHLF 310 320 330 340 350 360 PLALLCHDIM PPPSQVEIEI GEKRVIAFNG AGLSVAPEIS FEEIAATHKN PEEVREAYSK 370 380 390 ALFDSVAMQY NVLKTAISGK QGLGASTADV SLSQPW

References

[1]	"Cloning and nucleotide sequence of cDNA for the plastid glycerol-3-phosphate acyltransferase from squash." Ishizaki O., Nishida I., Agata K., Eguchi G., Murata N. FEBS Lett. 238:424-430(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: cv. Shirakikuza. Tissue: Cotyledon.
[2]	"Properties of the plastidial acyl-(acyl-carrier-protein): glycerol-3-phosphate acyltransferase from the chilling-sensitive plant squash (Cucurbita moschata)." Frentzen M., Nishida I., Murata N. Plant Cell Physiol. 28:1195-1201(1987) Cited for: CHARACTERIZATION.
[3]	"Analysis of the structure, substrate specificity, and mechanism of squash glycerol-3-phosphate (1)-acyltransferase." Turnbull A.P., Rafferty J.B., Sedelnikova S.E., Slabas A.R., Schierer T.P., Kroon J.T.M., Simon J.W., Fawcett T., Nishida I., Murata N., Rice D.W. Structure 9:347-353(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 32-396.
[4]	"Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea." Tamada T., Feese M.D., Ferri S.R., Kato Y., Yajima R., Toguri T., Kuroki R. Acta Crystallogr. D 60:13-21(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 32-396.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00771 mRNA. Translation: CAA68740.1.

PIR

S01660.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IUQ	X-ray	1.55	A	32-396	[»]
1K30	X-ray	1.90	A	32-396	[»]

ProteinModelPortal

P10349.

SMR

P10349. Positions 31-396.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P10349.

UniPathway

UPA00557; UER00612.

Family and domain databases

Gene3D

1.10.1200.50. 1 hit.

InterPro

IPR016222. G3P_O-acylTrfase_chlp.
IPR023083. G3P_O-acylTrfase_N.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]

Pfam

PF01553. Acyltransferase. 1 hit.
[Graphical view]

PIRSF

PIRSF000431. Glycerol-3-P_O-acyltransfrase. 1 hit.

SMART

SM00563. PlsC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P10349.

Entry information

Entry name

PLSB_CUCMO

Accession

Primary (citable) accession number: P10349

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program