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P49078

- ASNS1_ARATH

UniProt

P49078 - ASNS1_ARATH

Protein

Asparagine synthetase [glutamine-hydrolyzing] 1

Gene

ASN1

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 117 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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: TAIR
    2. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. asparagine biosynthetic process Source: UniProtKB
    2. cellular amino acid catabolic process Source: TAIR
    3. cellular response to sucrose starvation Source: TAIR
    4. glutamine metabolic process Source: UniProtKB-KW
    5. L-asparagine biosynthetic process Source: UniProtKB-UniPathway
    6. response to absence of light Source: TAIR
    7. response to fructose Source: TAIR
    8. response to glucose Source: TAIR
    9. response to sucrose Source: TAIR

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Amino-acid biosynthesis, Asparagine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciARA:GQT-1413-MONOMER.
    ARA:GQT-2583-MONOMER.
    UniPathwayiUPA00134; UER00195.

    Protein family/group databases

    MEROPSiC44.976.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Asparagine synthetase [glutamine-hydrolyzing] 1 (EC:6.3.5.4)
    Alternative name(s):
    Glutamine-dependent asparagine synthetase 1
    Protein DARK INDUCIBLE 6
    Gene namesi
    Name:ASN1
    Synonyms:DIN6
    Ordered Locus Names:At3g47340
    ORF Names:T21L8.90
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G47340.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 584583Asparagine synthetase [glutamine-hydrolyzing] 1PRO_0000056919Add
    BLAST

    Proteomic databases

    PaxDbiP49078.
    PRIDEiP49078.

    Expressioni

    Inductioni

    By dark. Down-regulated by light and sucrose.1 Publication

    Gene expression databases

    ArrayExpressiP49078.
    GenevestigatoriP49078.

    Structurei

    3D structure databases

    ProteinModelPortaliP49078.
    SMRiP49078. Positions 4-517.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 185184Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
    BLAST
    Domaini193 – 516324Asparagine synthetaseAdd
    BLAST

    Region

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

    Sequence similaritiesi

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

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiCOG0367.
    HOGENOMiHOG000027493.
    InParanoidiP49078.
    KOiK01953.
    OMAiDFINTAM.
    PhylomeDBiP49078.

    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]

    Sequencei

    Sequence statusi: Complete.

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

    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: P49078-1) [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 SDDSQAKRVR VLELSRRLRH RGPDWSGLYQ NGDNYLAHQR    50
    LAVIDPASGD QPLFNEDKTI VVTVNGEIYN HEELRKRLKN HKFRTGSDCE 100
    VIAHLYEEYG VDFVDMLDGI FSFVLLDTRD NSFMVARDAI GVTSLYIGWG 150
    LDGSVWISSE MKGLNDDCEH FETFPPGHFY SSKLGGFKQW YNPPWFNESV 200
    PSTPYEPLAI RRAFENAVIK RLMTDVPFGV LLSGGLDSSL VASITARHLA 250
    GTKAAKQWGP QLHSFCVGLE GSPDLKAGKE VAEYLGTVHH EFHFSVQDGI 300
    DAIEDVIYHV ETYDVTTIRA STPMFLMSRK IKSLGVKMVL SGEGADEIFG 350
    GYLYFHKAPN KKEFHQETCR KIKALHKYDC LRANKSTSAF GLEARVPFLD 400
    KDFINTAMSL DPESKMIKPE EGRIEKWVLR RAFDDEERPY LPKHILYRQK 450
    EQFSDGVGYS WIDGLKDHAA QNVNDKMMSN AGHIFPHNTP NTKEAYYYRM 500
    IFERFFPQNS ARLTVPGGAT VACSTAKAVE WDASWSNNMD PSGRAAIGVH 550
    LSAYDGKNVA LTIPPLKAID NMPMMMGQGV VIQS 584
    Length:584
    Mass (Da):65,621
    Last modified:January 23, 2007 - v2
    Checksum:i071910E4C6D02433
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29083 mRNA. Translation: AAA74359.1.
    AL096860 Genomic DNA. Translation: CAB51206.1.
    CP002686 Genomic DNA. Translation: AEE78264.1.
    AF419557 mRNA. Translation: AAL31889.1.
    AY072214 mRNA. Translation: AAL60035.1.
    AY096592 mRNA. Translation: AAM20242.1.
    PIRiT12989.
    RefSeqiNP_190318.1. NM_114602.3. [P49078-1]
    UniGeneiAt.20782.

    Genome annotation databases

    EnsemblPlantsiAT3G47340.1; AT3G47340.1; AT3G47340. [P49078-1]
    GeneIDi823888.
    KEGGiath:AT3G47340.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29083 mRNA. Translation: AAA74359.1 .
    AL096860 Genomic DNA. Translation: CAB51206.1 .
    CP002686 Genomic DNA. Translation: AEE78264.1 .
    AF419557 mRNA. Translation: AAL31889.1 .
    AY072214 mRNA. Translation: AAL60035.1 .
    AY096592 mRNA. Translation: AAM20242.1 .
    PIRi T12989.
    RefSeqi NP_190318.1. NM_114602.3. [P49078-1 ]
    UniGenei At.20782.

    3D structure databases

    ProteinModelPortali P49078.
    SMRi P49078. Positions 4-517.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C44.976.

    Proteomic databases

    PaxDbi P49078.
    PRIDEi P49078.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G47340.1 ; AT3G47340.1 ; AT3G47340 . [P49078-1 ]
    GeneIDi 823888.
    KEGGi ath:AT3G47340.

    Organism-specific databases

    TAIRi AT3G47340.

    Phylogenomic databases

    eggNOGi COG0367.
    HOGENOMi HOG000027493.
    InParanoidi P49078.
    KOi K01953.
    OMAi DFINTAM.
    PhylomeDBi P49078.

    Enzyme and pathway databases

    UniPathwayi UPA00134 ; UER00195 .
    BioCyci ARA:GQT-1413-MONOMER.
    ARA:GQT-2583-MONOMER.

    Gene expression databases

    ArrayExpressi P49078.
    Genevestigatori P49078.

    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. "Metabolic regulation of the gene encoding glutamine-dependent asparagine synthetase in Arabidopsis thaliana."
      Lam H.M., Peng S.S., Coruzzi G.M.
      Plant Physiol. 106:1347-1357(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [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.
    5. "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: TISSUE SPECIFICITY, INDUCTION.
    6. "Overexpression of the ASN1 gene enhances nitrogen status in seeds of Arabidopsis."
      Lam H.M., Wong P., Chan H.K., Yam K.M., Chen L., Chow C.M., Coruzzi G.M.
      Plant Physiol. 132:926-935(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiASNS1_ARATH
    AccessioniPrimary (citable) accession number: P49078
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Plants over-expressing ASN1 have increased content of free amino acids (mainly Asn) in flowers, siliques and seeds.1 Publication

    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