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P10349

- PLSB_CUCMO

UniProt

P10349 - PLSB_CUCMO

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
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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

    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 stroma Source: UniProtKB-SubCell

    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.

    P10349-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAELIQDKES AQSAATAAAA SSGYERRNEP AHSRKFLDVR SEEELLSCIK    50
    KETEAGKLPP NVAAGMEELY QNYRNAVIES GNPKADEIVL SNMTVALDRI 100
    LLDVEDPFVF SSHHKAIREP FDYYIFGQNY IRPLIDFGNS FVGNLSLFKD 150
    IEEKLQQGHN VVLISNHQTE ADPAIISLLL EKTNPYIAEN TIFVAGDRVL 200
    ADPLCKPFSI GRNLICVYSK KHMFDIPELT ETKRKANTRS LKEMALLLRG 250
    GSQLIWIAPS GGRDRPDPST GEWYPAPFDA SSVDNMRRLI QHSDVPGHLF 300
    PLALLCHDIM PPPSQVEIEI GEKRVIAFNG AGLSVAPEIS FEEIAATHKN 350
    PEEVREAYSK ALFDSVAMQY NVLKTAISGK QGLGASTADV SLSQPW 396
    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 1, 2014
    This is version 91 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