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P54887

- P5CS1_ARATH

UniProt

P54887 - P5CS1_ARATH

Protein

Delta-1-pyrroline-5-carboxylate synthase A

Gene

P5CSA

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    P5CS plays a key role in proline biosynthesis, leading to osmoregulation in plants.

    Catalytic activityi

    ATP + L-glutamate = ADP + L-glutamate 5-phosphate.
    L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei60 – 601SubstrateBy similarity
    Binding sitei157 – 1571SubstrateBy similarity
    Binding sitei176 – 1761Substrate; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi196 – 1972ATPBy similarity
    Nucleotide bindingi236 – 2427ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. delta1-pyrroline-5-carboxylate synthetase activity Source: TAIR
    3. glutamate 5-kinase activity Source: UniProtKB-EC
    4. glutamate-5-semialdehyde dehydrogenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. hyperosmotic salinity response Source: TAIR
    2. L-proline biosynthetic process Source: UniProtKB-UniPathway
    3. pollen development Source: TAIR
    4. proline biosynthetic process Source: TAIR
    5. response to oxidative stress Source: TAIR
    6. response to salt stress Source: TAIR
    7. response to water deprivation Source: TAIR
    8. root development Source: TAIR

    Keywords - Molecular functioni

    Kinase, Oxidoreductase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Proline biosynthesis

    Keywords - Ligandi

    ATP-binding, NADP, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciARA:AT2G39800-MONOMER.
    ARA:GQT-2788-MONOMER.
    ARA:GQT-2789-MONOMER.
    ARA:GQT-2790-MONOMER.
    MetaCyc:AT2G39800-MONOMER.
    UniPathwayiUPA00098; UER00359.
    UPA00098; UER00360.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Delta-1-pyrroline-5-carboxylate synthase A
    Short name:
    P5CS A
    Including the following 2 domains:
    Glutamate 5-kinase (EC:2.7.2.11)
    Short name:
    GK
    Alternative name(s):
    Gamma-glutamyl kinase
    Gamma-glutamyl phosphate reductase (EC:1.2.1.41)
    Short name:
    GPR
    Alternative name(s):
    Glutamate-5-semialdehyde dehydrogenase
    Glutamyl-gamma-semialdehyde dehydrogenase
    Gene namesi
    Name:P5CSA
    Synonyms:P5CS1
    Ordered Locus Names:At2g39800
    ORF Names:T5I7.10
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 2

    Organism-specific databases

    TAIRiAT2G39800.

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. cytoplasm Source: TAIR
    3. membrane Source: TAIR

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 717717Delta-1-pyrroline-5-carboxylate synthase APRO_0000109772Add
    BLAST

    Proteomic databases

    PaxDbiP54887.
    PRIDEiP54887.

    Expressioni

    Gene expression databases

    GenevestigatoriP54887.

    Interactioni

    Protein-protein interaction databases

    BioGridi3904. 6 interactions.
    IntActiP54887. 6 interactions.
    STRINGi3702.AT2G39800.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliP54887.
    SMRiP54887. Positions 13-284, 302-715.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 296296Glutamate 5-kinaseAdd
    BLAST
    Regioni297 – 717421Gamma-glutamyl phosphate reductaseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the glutamate 5-kinase family.Curated
    In the C-terminal section; belongs to the gamma-glutamyl phosphate reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0014.
    HOGENOMiHOG000246357.
    InParanoidiP54887.
    KOiK12657.
    OMAiFEARPDC.
    PhylomeDBiP54887.

    Family and domain databases

    Gene3Di3.40.1160.10. 1 hit.
    3.40.309.10. 1 hit.
    3.40.605.10. 2 hits.
    HAMAPiMF_00412. ProA.
    MF_00456. ProB.
    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR001048. Asp/Glu/Uridylate_kinase.
    IPR000965. G-glutamylP_reductase.
    IPR020593. G-glutamylP_reductase_CS.
    IPR001057. Glu/AcGlu_kinase.
    IPR005715. Glu_5kinase/COase_Synthase.
    IPR019797. Glutamate_5-kinase_CS.
    IPR005766. P5_carboxy_syn.
    [Graphical view]
    PfamiPF00696. AA_kinase. 1 hit.
    PF00171. Aldedh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036429. P5C_syn. 1 hit.
    PRINTSiPR00474. GLU5KINASE.
    SUPFAMiSSF53633. SSF53633. 1 hit.
    SSF53720. SSF53720. 1 hit.
    TIGRFAMsiTIGR01092. P5CS. 1 hit.
    TIGR00407. proA. 1 hit.
    TIGR01027. proB. 1 hit.
    PROSITEiPS00902. GLUTAMATE_5_KINASE. 1 hit.
    PS01223. PROA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: A number of isoforms are produced. According to EST sequences.

    Isoform 1 (identifier: P54887-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEELDRSRAF ARDVKRIVVK VGTAVVTGKG GRLALGRLGA LCEQLAELNS    50
    DGFEVILVSS GAVGLGRQRL RYRQLVNSSF ADLQKPQTEL DGKACAGVGQ 100
    SSLMAYYETM FDQLDVTAAQ LLVNDSSFRD KDFRKQLNET VKSMLDLRVI 150
    PIFNENDAIS TRRAPYQDSS GIFWDNDSLA ALLALELKAD LLILLSDVEG 200
    LYTGPPSDPN SKLIHTFVKE KHQDEITFGD KSRLGRGGMT AKVKAAVNAA 250
    YAGIPVIITS GYSAENIDKV LRGLRVGTLF HQDARLWAPI TDSNARDMAV 300
    AARESSRKLQ ALSSEDRKKI LLDIADALEA NVTTIKAENE LDVASAQEAG 350
    LEESMVARLV MTPGKISSLA ASVRKLADME DPIGRVLKKT EVADGLVLEK 400
    TSSPLGVLLI VFESRPDALV QIASLAIRSG NGLLLKGGKE ARRSNAILHK 450
    VITDAIPETV GGKLIGLVTS REEIPDLLKL DDVIDLVIPR GSNKLVTQIK 500
    NTTKIPVLGH ADGICHVYVD KACDTDMAKR IVSDAKLDYP AACNAMETLL 550
    VHKDLEQNAV LNELIFALQS NGVTLYGGPR ASKILNIPEA RSFNHEYCAK 600
    ACTVEVVEDV YGAIDHIHRH GSAHTDCIVT EDHEVAELFL RQVDSAAVFH 650
    NASTRFSDGF RFGLGAEVGV STGRIHARGP VGVEGLLTTR WIMRGKGQVV 700
    DGDNGIVYTH QDIPIQA 717
    Length:717
    Mass (Da):77,702
    Last modified:October 1, 1996 - v1
    Checksum:iDF2B296362351A78
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 421C → F in BAA06864. (PubMed:7773306)Curated
    Sequence conflicti54 – 541E → K in BAA06864. (PubMed:7773306)Curated
    Sequence conflicti381 – 3811D → E in BAA06864. (PubMed:7773306)Curated
    Sequence conflicti467 – 4671L → F in BAA06864. (PubMed:7773306)Curated
    Sequence conflicti676 – 6761H → Y in BAA06864. (PubMed:7773306)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89414 Genomic DNA. Translation: CAA61593.1.
    X86777 mRNA. Translation: CAA60446.1.
    X87330 mRNA. Translation: CAA60740.1.
    D32138 mRNA. Translation: BAA06864.1.
    AC003000 Genomic DNA. Translation: AAB87129.1.
    CP002685 Genomic DNA. Translation: AEC09729.1.
    CP002685 Genomic DNA. Translation: AEC09730.1.
    AF424633 mRNA. Translation: AAL11626.1.
    AY113046 mRNA. Translation: AAM47354.1.
    AY150430 mRNA. Translation: AAN12972.1.
    PIRiS66637.
    T50685.
    RefSeqiNP_001189714.1. NM_001202785.1. [P54887-1]
    NP_181510.1. NM_129539.2. [P54887-1]
    UniGeneiAt.20482.

    Genome annotation databases

    EnsemblPlantsiAT2G39800.1; AT2G39800.1; AT2G39800. [P54887-1]
    AT2G39800.4; AT2G39800.4; AT2G39800. [P54887-1]
    GeneIDi818566.
    KEGGiath:AT2G39800.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89414 Genomic DNA. Translation: CAA61593.1 .
    X86777 mRNA. Translation: CAA60446.1 .
    X87330 mRNA. Translation: CAA60740.1 .
    D32138 mRNA. Translation: BAA06864.1 .
    AC003000 Genomic DNA. Translation: AAB87129.1 .
    CP002685 Genomic DNA. Translation: AEC09729.1 .
    CP002685 Genomic DNA. Translation: AEC09730.1 .
    AF424633 mRNA. Translation: AAL11626.1 .
    AY113046 mRNA. Translation: AAM47354.1 .
    AY150430 mRNA. Translation: AAN12972.1 .
    PIRi S66637.
    T50685.
    RefSeqi NP_001189714.1. NM_001202785.1. [P54887-1 ]
    NP_181510.1. NM_129539.2. [P54887-1 ]
    UniGenei At.20482.

    3D structure databases

    ProteinModelPortali P54887.
    SMRi P54887. Positions 13-284, 302-715.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 3904. 6 interactions.
    IntActi P54887. 6 interactions.
    STRINGi 3702.AT2G39800.1-P.

    Proteomic databases

    PaxDbi P54887.
    PRIDEi P54887.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G39800.1 ; AT2G39800.1 ; AT2G39800 . [P54887-1 ]
    AT2G39800.4 ; AT2G39800.4 ; AT2G39800 . [P54887-1 ]
    GeneIDi 818566.
    KEGGi ath:AT2G39800.

    Organism-specific databases

    TAIRi AT2G39800.

    Phylogenomic databases

    eggNOGi COG0014.
    HOGENOMi HOG000246357.
    InParanoidi P54887.
    KOi K12657.
    OMAi FEARPDC.
    PhylomeDBi P54887.

    Enzyme and pathway databases

    UniPathwayi UPA00098 ; UER00359 .
    UPA00098 ; UER00360 .
    BioCyci ARA:AT2G39800-MONOMER.
    ARA:GQT-2788-MONOMER.
    ARA:GQT-2789-MONOMER.
    ARA:GQT-2790-MONOMER.
    MetaCyc:AT2G39800-MONOMER.

    Gene expression databases

    Genevestigatori P54887.

    Family and domain databases

    Gene3Di 3.40.1160.10. 1 hit.
    3.40.309.10. 1 hit.
    3.40.605.10. 2 hits.
    HAMAPi MF_00412. ProA.
    MF_00456. ProB.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR001048. Asp/Glu/Uridylate_kinase.
    IPR000965. G-glutamylP_reductase.
    IPR020593. G-glutamylP_reductase_CS.
    IPR001057. Glu/AcGlu_kinase.
    IPR005715. Glu_5kinase/COase_Synthase.
    IPR019797. Glutamate_5-kinase_CS.
    IPR005766. P5_carboxy_syn.
    [Graphical view ]
    Pfami PF00696. AA_kinase. 1 hit.
    PF00171. Aldedh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036429. P5C_syn. 1 hit.
    PRINTSi PR00474. GLU5KINASE.
    SUPFAMi SSF53633. SSF53633. 1 hit.
    SSF53720. SSF53720. 1 hit.
    TIGRFAMsi TIGR01092. P5CS. 1 hit.
    TIGR00407. proA. 1 hit.
    TIGR01027. proB. 1 hit.
    PROSITEi PS00902. GLUTAMATE_5_KINASE. 1 hit.
    PS01223. PROA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation, characterization, and chromosomal location of a gene encoding the delta 1-pyrroline-5-carboxylate synthetase in Arabidopsis thaliana."
      Savoure A., Jaoua S., Hua X.J., Ardiles W., van Montagu M., Verbruggen N.
      FEBS Lett. 372:13-19(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: cv. Columbia.
    2. "Differential expression of two P5CS genes controlling proline accumulation during salt-stress requires ABA and is regulated by ABA1, ABI1 and AXR2 in Arabidopsis."
      Strizhov N., Abraham E., Oekresz L., Blickling S., Zilberstein A., Schell J., Koncz C., Szabados L.
      Plant J. 12:557-569(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    3. "Correlation between the induction of a gene for delta 1-pyrroline-5-carboxylate synthetase and the accumulation of proline in Arabidopsis thaliana under osmotic stress."
      Yoshiba Y., Kiyosue T., Katagiri T., Ueda H., Mizoguchi T., Yamaguchi-Shinozaki K., Wada K., Harada Y., Shinozaki K.
      Plant J. 7:751-760(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    5. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    7. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
      Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
      Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiP5CS1_ARATH
    AccessioniPrimary (citable) accession number: P54887
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3