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Protein

Glycerol-3-phosphate acyltransferase, chloroplastic

Gene
N/A
Organism
Cucurbita moschata (Winter crookneck squash) (Cucurbita pepo var. moschata)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.

Pathwayi: CDP-diacylglycerol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glycerol-3-phosphate acyltransferase, chloroplastic
  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

BRENDAi2.3.1.15. 1739.
SABIO-RKP10349.
UniPathwayiUPA00557; UER00612.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate acyltransferase, chloroplastic (EC:2.3.1.15)
Short name:
GPAT
OrganismiCucurbita moschata (Winter crookneck squash) (Cucurbita pepo var. moschata)
Taxonomic identifieri3662 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeCucurbiteaeCucurbita

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 28ChloroplastAdd BLAST28
ChainiPRO_000002469629 – 396Glycerol-3-phosphate acyltransferase, chloroplasticAdd BLAST368

Proteomic databases

PRIDEiP10349.

Structurei

Secondary structure

1396
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi35 – 38Combined sources4
Helixi42 – 54Combined sources13
Helixi60 – 79Combined sources20
Helixi85 – 105Combined sources21
Beta strandi112 – 114Combined sources3
Beta strandi119 – 121Combined sources3
Helixi123 – 131Combined sources9
Helixi132 – 134Combined sources3
Helixi137 – 139Combined sources3
Beta strandi141 – 143Combined sources3
Helixi145 – 156Combined sources12
Beta strandi160 – 165Combined sources6
Helixi172 – 180Combined sources9
Turni181 – 183Combined sources3
Helixi185 – 190Combined sources6
Beta strandi192 – 195Combined sources4
Helixi198 – 201Combined sources4
Turni203 – 205Combined sources3
Helixi206 – 210Combined sources5
Beta strandi212 – 216Combined sources5
Helixi220 – 222Combined sources3
Helixi227 – 229Combined sources3
Helixi230 – 250Combined sources21
Beta strandi254 – 257Combined sources4
Turni268 – 270Combined sources3
Helixi280 – 291Combined sources12
Beta strandi293 – 295Combined sources3
Beta strandi297 – 305Combined sources9
Helixi307 – 309Combined sources3
Helixi315 – 319Combined sources5
Beta strandi332 – 335Combined sources4
Helixi341 – 346Combined sources6
Beta strandi348 – 350Combined sources3
Helixi351 – 376Combined sources26
Turni377 – 379Combined sources3
Helixi382 – 385Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IUQX-ray1.55A32-396[»]
1K30X-ray1.90A32-396[»]
ProteinModelPortaliP10349.
SMRiP10349.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10349.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi167 – 172HXXXXD 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.

Sequence similaritiesi

Belongs to the GPAT/DAPAT family.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di1.10.1200.50. 1 hit.
InterProiIPR016222. G3P_O-acylTrfase_chlp.
IPR023083. G3P_O-acylTrfase_N.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
PF14829. GPAT_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000431. Glycerol-3-P_O-acyltransfrase. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10349-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAELIQDKES AQSAATAAAA SSGYERRNEP AHSRKFLDVR SEEELLSCIK
60 70 80 90 100
KETEAGKLPP NVAAGMEELY QNYRNAVIES GNPKADEIVL SNMTVALDRI
110 120 130 140 150
LLDVEDPFVF SSHHKAIREP FDYYIFGQNY IRPLIDFGNS FVGNLSLFKD
160 170 180 190 200
IEEKLQQGHN VVLISNHQTE ADPAIISLLL EKTNPYIAEN TIFVAGDRVL
210 220 230 240 250
ADPLCKPFSI GRNLICVYSK KHMFDIPELT ETKRKANTRS LKEMALLLRG
260 270 280 290 300
GSQLIWIAPS GGRDRPDPST GEWYPAPFDA SSVDNMRRLI QHSDVPGHLF
310 320 330 340 350
PLALLCHDIM PPPSQVEIEI GEKRVIAFNG AGLSVAPEIS FEEIAATHKN
360 370 380 390
PEEVREAYSK ALFDSVAMQY NVLKTAISGK QGLGASTADV SLSQPW
Length:396
Mass (Da):43,839
Last modified:July 1, 1989 - v1
Checksum:iCB96E8C057B88112
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00771 mRNA. Translation: CAA68740.1.
PIRiS01660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00771 mRNA. Translation: CAA68740.1.
PIRiS01660.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IUQX-ray1.55A32-396[»]
1K30X-ray1.90A32-396[»]
ProteinModelPortaliP10349.
SMRiP10349.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP10349.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00557; UER00612.
BRENDAi2.3.1.15. 1739.
SABIO-RKP10349.

Miscellaneous databases

EvolutionaryTraceiP10349.

Family and domain databases

Gene3Di1.10.1200.50. 1 hit.
InterProiIPR016222. G3P_O-acylTrfase_chlp.
IPR023083. G3P_O-acylTrfase_N.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
PF14829. GPAT_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000431. Glycerol-3-P_O-acyltransfrase. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPLSB_CUCMO
AccessioniPrimary (citable) accession number: P10349
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

May represent a 5'-truncated sequence in which part of the leader sequence is missing.Curated

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.