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Q9LV77

- ASNS2_ARATH

UniProt

Q9LV77 - ASNS2_ARATH

Protein

Asparagine synthetase [glutamine-hydrolyzing] 2

Gene

ASN2

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 93 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Essential for nitrogen assimilation, distribution and remobilization within the plant via the phloem.1 Publication

    Catalytic activityi

    ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei2 – 21For GATase activityBy similarity
    Binding sitei98 – 981GlutamineBy similarity
    Binding sitei231 – 2311ATP; via carbonyl oxygenBy similarity
    Binding sitei267 – 2671ATP; via amide nitrogen and carbonyl oxygenBy similarity
    Sitei343 – 3431Important for beta-aspartyl-AMP intermediate formationBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi341 – 3422ATPBy similarity

    GO - Molecular functioni

    1. asparagine synthase (glutamine-hydrolyzing) activity Source: UniProtKB-EC
    2. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. glutamine metabolic process Source: UniProtKB-KW
    2. L-asparagine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Amino-acid biosynthesis, Asparagine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciARA:GQT-858-MONOMER.
    UniPathwayiUPA00134.

    Protein family/group databases

    MEROPSiC44.976.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Asparagine synthetase [glutamine-hydrolyzing] 2 (EC:6.3.5.4)
    Alternative name(s):
    Glutamine-dependent asparagine synthetase 2
    Gene namesi
    Name:ASN2
    Ordered Locus Names:At5g65010
    ORF Names:MXK3.25
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G65010.

    Pathology & Biotechi

    Disruption phenotypei

    Pale green leaf phenotype and reduction of biomass in mature plants. Increased levels of asparagine, proline and ammonium in response to salt treatment.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 578577Asparagine synthetase [glutamine-hydrolyzing] 2PRO_0000420840Add
    BLAST

    Proteomic databases

    PRIDEiQ9LV77.
    ProMEXiQ9LV77.

    Expressioni

    Tissue specificityi

    Expressed in the vascular region adjacent to leaf mesophyll cells in the companion cell-sieve tube element complex.2 Publications

    Inductioni

    By light and sucrose. Down-regulated by dark.3 Publications

    Gene expression databases

    GenevestigatoriQ9LV77.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT5G65010.2-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LV77.
    SMRiQ9LV77. Positions 18-517.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 185184Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
    BLAST
    Domaini210 – 450241Asparagine synthetaseAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 545Glutamine bindingBy similarity
    Regioni75 – 773Glutamine bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi559 – 5657Poly-Ala

    Sequence similaritiesi

    Contains 1 asparagine synthetase domain.Curated
    Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    HOGENOMiHOG000027493.
    InParanoidiQ9LV77.
    KOiK01953.
    OMAiICGELRF.
    PhylomeDBiQ9LV77.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    3.60.20.10. 1 hit.
    InterProiIPR006426. Asn_synth_AEB.
    IPR001962. Asn_synthase.
    IPR017932. GATase_2_dom.
    IPR000583. GATase_dom.
    IPR029055. Ntn_hydrolases_N.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF00733. Asn_synthase. 1 hit.
    PF13537. GATase_7. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001589. Asn_synthetase_glu-h. 1 hit.
    SUPFAMiSSF56235. SSF56235. 1 hit.
    TIGRFAMsiTIGR01536. asn_synth_AEB. 1 hit.
    PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9LV77-1) [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

    MCGILAVLGC IDNSQAKRSR IIELSRRLRH RGPDWSGLHC YEDCYLAHER    50
    LAIIDPTSGD QPLYNEDKTV AVTVNGEIYN HKILREKLKS HQFRTGSDCE 100
    VIAHLYEEHG EEFIDMLDGM FAFVLLDTRD KSFIAARDAI GITPLYIGWG 150
    LDGSVWFASE MKALSDDCEQ FMSFPPGHIY SSKQGGLRRW YNPPWYNEQV 200
    PSTPYDPLVL RNAFEKAVIK RLMTDVPFGV LLSGGLDSSL VAAVALRHLE 250
    KSEAARQWGS QLHTFCIGLQ GSPDLKAGRE VADYLGTRHH EFQFTVQDGI 300
    DAIEEVIYHI ETYDVTTIRA STPMFLMSRK IKSLGVKMVL SGEGSDEILG 350
    GYLYFHKAPN KKEFHEETCR KIKALHQFDC LRANKSTSAW GVEARVPFLD 400
    KEFLNVAMSI DPEWKLIKPD LGRIEKWVLR NAFDDEERPY LPKHILYRQK 450
    EQFSDGVGYS WIDGLKDHAN KHVSDTMLSN ASFVFPDNTP LTKEAYYYRT 500
    IFEKFFPKSA ARATVPGGPS IACSTAKAVE WDATWSKNLD PSGRAALGVH 550
    VAAYEEDKAA AAAKAGSDLV DPLPKNGT 578
    Length:578
    Mass (Da):65,030
    Last modified:October 1, 2000 - v1
    Checksum:iCAEAD8DC90F3A773
    GO
    Isoform 2 (identifier: Q9LV77-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         508-508: K → KQ

    Note: Derived from EST data. No experimental confirmation available.

    Show »
    Length:579
    Mass (Da):65,158
    Checksum:iAF6CE3E95A30A9F5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti484 – 4841V → F in AAC72837. (PubMed:9881155)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei508 – 5081K → KQ in isoform 2. CuratedVSP_044714

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF095453 mRNA. Translation: AAC72837.1.
    AB019236 Genomic DNA. Translation: BAA97313.1.
    CP002688 Genomic DNA. Translation: AED97984.1.
    CP002688 Genomic DNA. Translation: AED97985.1.
    AF367340 mRNA. Translation: AAK32927.1.
    AY124866 mRNA. Translation: AAM70575.1.
    RefSeqiNP_201306.2. NM_125900.2. [Q9LV77-2]
    NP_851272.1. NM_180941.2. [Q9LV77-1]
    UniGeneiAt.67717.
    At.7860.

    Genome annotation databases

    EnsemblPlantsiAT5G65010.1; AT5G65010.1; AT5G65010. [Q9LV77-1]
    GeneIDi836625.
    KEGGiath:AT5G65010.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF095453 mRNA. Translation: AAC72837.1 .
    AB019236 Genomic DNA. Translation: BAA97313.1 .
    CP002688 Genomic DNA. Translation: AED97984.1 .
    CP002688 Genomic DNA. Translation: AED97985.1 .
    AF367340 mRNA. Translation: AAK32927.1 .
    AY124866 mRNA. Translation: AAM70575.1 .
    RefSeqi NP_201306.2. NM_125900.2. [Q9LV77-2 ]
    NP_851272.1. NM_180941.2. [Q9LV77-1 ]
    UniGenei At.67717.
    At.7860.

    3D structure databases

    ProteinModelPortali Q9LV77.
    SMRi Q9LV77. Positions 18-517.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT5G65010.2-P.

    Protein family/group databases

    MEROPSi C44.976.

    Proteomic databases

    PRIDEi Q9LV77.
    ProMEXi Q9LV77.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G65010.1 ; AT5G65010.1 ; AT5G65010 . [Q9LV77-1 ]
    GeneIDi 836625.
    KEGGi ath:AT5G65010.

    Organism-specific databases

    TAIRi AT5G65010.

    Phylogenomic databases

    HOGENOMi HOG000027493.
    InParanoidi Q9LV77.
    KOi K01953.
    OMAi ICGELRF.
    PhylomeDBi Q9LV77.

    Enzyme and pathway databases

    UniPathwayi UPA00134 .
    BioCyci ARA:GQT-858-MONOMER.

    Gene expression databases

    Genevestigatori Q9LV77.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    3.60.20.10. 1 hit.
    InterProi IPR006426. Asn_synth_AEB.
    IPR001962. Asn_synthase.
    IPR017932. GATase_2_dom.
    IPR000583. GATase_dom.
    IPR029055. Ntn_hydrolases_N.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF00733. Asn_synthase. 1 hit.
    PF13537. GATase_7. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001589. Asn_synthetase_glu-h. 1 hit.
    SUPFAMi SSF56235. SSF56235. 1 hit.
    TIGRFAMsi TIGR01536. asn_synth_AEB. 1 hit.
    PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Reciprocal regulation of distinct asparagine synthetase genes by light and metabolites in Arabidopsis thaliana."
      Lam H.M., Hsieh M.H., Coruzzi G.
      Plant J. 16:345-353(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION.
    2. "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
      Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
      DNA Res. 7:31-63(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] (ISOFORM 1).
      Strain: cv. Columbia.
    5. "Correlation of ASN2 gene expression with ammonium metabolism in Arabidopsis."
      Wong H.K., Chan H.K., Coruzzi G.M., Lam H.M.
      Plant Physiol. 134:332-338(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    6. "An Arabidopsis mutant disrupted in ASN2 encoding asparagine synthetase 2 exhibits low salt stress tolerance."
      Maaroufi-Dguimi H., Debouba M., Gaufichon L., Clement G., Gouia H., Hajjaji A., Suzuki A.
      Plant Physiol. Biochem. 49:623-628(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    7. "Arabidopsis thaliana ASN2 encoding asparagine synthetase is involved in the control of nitrogen assimilation and export during vegetative growth."
      Gaufichon L., Masclaux-Daubresse C., Tcherkez G., Reisdorf-Cren M., Sakakibara Y., Hase T., Clement G., Avice J.C., Grandjean O., Marmagne A., Boutet-Mercey S., Azzopardi M., Soulay F., Suzuki A.
      Plant Cell Environ. 36:328-342(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiASNS2_ARATH
    AccessioniPrimary (citable) accession number: Q9LV77
    Secondary accession number(s): F4KGG8, Q9ZST6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2013
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 93 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, 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