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P10349

- PLSB_CUCMO

UniProt

P10349 - PLSB_CUCMO

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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: 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

GO - Molecular functioni

  1. glycerol-3-phosphate O-acyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

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

  1. chloroplast Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828ChloroplastAdd
BLAST
Chaini29 – 396368Glycerol-3-phosphate acyltransferase, chloroplasticPRO_0000024696Add
BLAST

Structurei

Secondary structure

1
396
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 384
Helixi42 – 5413
Helixi60 – 7920
Helixi85 – 10521
Beta strandi112 – 1143
Beta strandi119 – 1213
Helixi123 – 1319
Helixi132 – 1343
Helixi137 – 1393
Beta strandi141 – 1433
Helixi145 – 15612
Beta strandi160 – 1656
Helixi172 – 1809
Turni181 – 1833
Helixi185 – 1906
Beta strandi192 – 1954
Helixi198 – 2014
Turni203 – 2053
Helixi206 – 2105
Beta strandi212 – 2165
Helixi220 – 2223
Helixi227 – 2293
Helixi230 – 25021
Beta strandi254 – 2574
Turni268 – 2703
Helixi280 – 29112
Beta strandi293 – 2953
Beta strandi297 – 3059
Helixi307 – 3093
Helixi315 – 3195
Beta strandi332 – 3354
Helixi341 – 3466
Beta strandi348 – 3503
Helixi351 – 37626
Turni377 – 3793
Helixi382 – 3854

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IUQX-ray1.55A32-396[»]
1K30X-ray1.90A32-396[»]
ProteinModelPortaliP10349.
SMRiP10349. Positions 31-396.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10349.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi167 – 1726HXXXXD motif

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 [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:
EMBL
GenBank
DDBJ
Links Updated
Y00771 mRNA. Translation: CAA68740.1.
PIRiS01660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00771 mRNA. Translation: CAA68740.1 .
PIRi S01660.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IUQ X-ray 1.55 A 32-396 [» ]
1K30 X-ray 1.90 A 32-396 [» ]
ProteinModelPortali P10349.
SMRi P10349. Positions 31-396.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00557 ; UER00612 .
SABIO-RK P10349.

Miscellaneous databases

EvolutionaryTracei P10349.

Family and domain databases

Gene3Di 1.10.1200.50. 1 hit.
InterProi IPR016222. G3P_O-acylTrfase_chlp.
IPR023083. G3P_O-acylTrfase_N.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view ]
Pfami PF01553. Acyltransferase. 1 hit.
PF14829. GPAT_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000431. Glycerol-3-P_O-acyltransfrase. 1 hit.
SMARTi SM00563. PlsC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

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: October 29, 2014
This is version 92 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

External Data

Dasty 3