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P54888

- P5CS2_ARATH

UniProt

P54888 - P5CS2_ARATH

Protein

Delta-1-pyrroline-5-carboxylate synthase B

Gene

P5CSB

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 121 (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. glutamate 5-kinase activity Source: UniProtKB-EC
    3. glutamate-5-semialdehyde dehydrogenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. embryo development ending in seed dormancy Source: TAIR
    2. L-proline biosynthetic process Source: UniProtKB-UniPathway
    3. pollen development Source: TAIR
    4. proline biosynthetic process 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:GQT-931-MONOMER.
    UniPathwayiUPA00098; UER00359.
    UPA00098; UER00360.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Delta-1-pyrroline-5-carboxylate synthase B
    Short name:
    P5CS B
    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:P5CSB
    Synonyms:P5CS2
    Ordered Locus Names:At3g55610
    ORF Names:F1I16_20
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G55610.

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. cytoplasm Source: TAIR
    3. cytosol Source: TAIR
    4. plasmodesma Source: TAIR

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 726726Delta-1-pyrroline-5-carboxylate synthase BPRO_0000109773Add
    BLAST

    Proteomic databases

    PaxDbiP54888.
    PRIDEiP54888.

    Expressioni

    Gene expression databases

    GenevestigatoriP54888.

    Interactioni

    Protein-protein interaction databases

    BioGridi10043. 2 interactions.
    IntActiP54888. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP54888.
    SMRiP54888. Positions 13-284, 302-718.
    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.
    InParanoidiP54888.
    KOiK12657.
    OMAiLLPWVQS.
    PhylomeDBiP54888.

    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.
    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.
    [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: P54888-1) [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

    MTEIDRSRAF AKDVKRIVVK VGTAVVTGKG GRLALGRLGA ICEQLAELNS    50
    DGFEVILVSS GAVGLGRQRL RYRQLVNSSF ADLQKPQMEL DGKACAGVGQ 100
    SSLMAYYETM FDQLDVTVAQ MLVTDSSFRD KDFRKQLSET VKAMLRMRVI 150
    PVFNENDAIS TRRAPYKDST GIFWDNDSLA ALLSLELKAD LLILLSDVEG 200
    LYTGPPSDST SKLIHTFIKE KHQDEITFGE KSKLGRGGMT AKVKAAVNAA 250
    YGGVPVIITS GYAAENISKV LRGLRVGTLF HQDAHLWAPV VDTTSRDMAV 300
    AARESSRKLQ ALSSEDRKQI LHDIANALEV NEKTIKAEND LDVAAAQEAG 350
    YEESLVARLV MKPGKISSLA ASVRQLAEME DPIGRVLKKT QVADDLILEK 400
    TSSPIGVLLI VFESRPDALV QIASLAIRSG NGLLLKGGKE ARRSNAILHK 450
    VITDAIPETV GGKLIGLVTS REEIPDLLKL DDVIDLVIPR GSNKLVSQIK 500
    NSTKIPVLGH ADGICHVYVD KSGKLDMAKR IVSDAKLDYP AACNAMETLL 550
    VHKDLEQNGF LDDLIYVLQT KGVTLYGGPR ASAKLNIPET KSFHHEYSSK 600
    ACTVEIVEDV YGAIDHIHQH GSAHTDCIVT EDSEVAEIFL RQVDSAAVFH 650
    NASTRFSDGF RFGLGAEVGI STSRIHARGP VGVEGLLTTR WIMRGKGQVV 700
    DGDNGIVYTH KDLPVLQRTE AVENGI 726
    Length:726
    Mass (Da):78,871
    Last modified:October 1, 1996 - v1
    Checksum:iE01446A6659021FF
    GO

    Sequence cautioni

    The sequence CAB81586.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X86778 Genomic DNA. Translation: CAA60447.1.
    Y09355 mRNA. Translation: CAA70527.1.
    AL161667 Genomic DNA. Translation: CAB81586.1. Sequence problems.
    CP002686 Genomic DNA. Translation: AEE79408.1.
    AY091766 mRNA. Translation: AAM10314.1.
    PIRiT47700.
    T50682. T50684.
    RefSeqiNP_191120.2. NM_115419.4. [P54888-1]
    UniGeneiAt.25196.

    Genome annotation databases

    EnsemblPlantsiAT3G55610.1; AT3G55610.1; AT3G55610. [P54888-1]
    GeneIDi824727.
    KEGGiath:AT3G55610.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X86778 Genomic DNA. Translation: CAA60447.1 .
    Y09355 mRNA. Translation: CAA70527.1 .
    AL161667 Genomic DNA. Translation: CAB81586.1 . Sequence problems.
    CP002686 Genomic DNA. Translation: AEE79408.1 .
    AY091766 mRNA. Translation: AAM10314.1 .
    PIRi T47700.
    T50682. T50684.
    RefSeqi NP_191120.2. NM_115419.4. [P54888-1 ]
    UniGenei At.25196.

    3D structure databases

    ProteinModelPortali P54888.
    SMRi P54888. Positions 13-284, 302-718.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 10043. 2 interactions.
    IntActi P54888. 2 interactions.

    Proteomic databases

    PaxDbi P54888.
    PRIDEi P54888.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G55610.1 ; AT3G55610.1 ; AT3G55610 . [P54888-1 ]
    GeneIDi 824727.
    KEGGi ath:AT3G55610.

    Organism-specific databases

    TAIRi AT3G55610.

    Phylogenomic databases

    eggNOGi COG0014.
    HOGENOMi HOG000246357.
    InParanoidi P54888.
    KOi K12657.
    OMAi LLPWVQS.
    PhylomeDBi P54888.

    Enzyme and pathway databases

    UniPathwayi UPA00098 ; UER00359 .
    UPA00098 ; UER00360 .
    BioCyci ARA:GQT-931-MONOMER.

    Gene expression databases

    Genevestigatori P54888.

    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.
    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.
    [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. "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 [GENOMIC DNA / MRNA].
      Strain: cv. Columbia.
    2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "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.

    Entry informationi

    Entry nameiP5CS2_ARATH
    AccessioniPrimary (citable) accession number: P54888
    Secondary accession number(s): Q9M061
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 121 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