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Q9LFU1

- ASNS3_ARATH

UniProt

Q9LFU1 - ASNS3_ARATH

Protein

Asparagine synthetase [glutamine-hydrolyzing] 3

Gene

ASN3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 89 (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.By similarity

    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. aspartate-ammonia ligase activity Source: TAIR
    3. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. asparagine biosynthetic process Source: TAIR
    2. glutamine metabolic process Source: UniProtKB-KW
    3. 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-424-MONOMER.
    UniPathwayiUPA00134.

    Protein family/group databases

    MEROPSiC44.976.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Asparagine synthetase [glutamine-hydrolyzing] 3 (EC:6.3.5.4)
    Alternative name(s):
    Glutamine-dependent asparagine synthetase 3
    Gene namesi
    Name:ASN3
    Ordered Locus Names:At5g10240
    ORF Names:F18D22.10, T31P16.230
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G10240.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: TAIR

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 578577Asparagine synthetase [glutamine-hydrolyzing] 3PRO_0000420841Add
    BLAST

    Proteomic databases

    PaxDbiQ9LFU1.
    PRIDEiQ9LFU1.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9LFU1.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT5G10240.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LFU1.
    SMRiQ9LFU1. 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

    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.
    InParanoidiQ9LFU1.
    KOiK01953.
    OMAiEKSEAAC.
    PhylomeDBiQ9LFU1.

    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: Q9LFU1-1) [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 VDNSQAKRSR IIELSRRLRH RGPDWSGLHC YEDCYLAHER    50
    LAIVDPTSGD QPLYNEDKTI AVTVNGEIYN HKALRENLKS HQFRTGSDCE 100
    VIAHLYEEHG EEFVDMLDGM FAFVLLDTRD KSFIAARDAI GITPLYIGWG 150
    LDGSVWFASE MKALSDDCEQ FMCFPPGHIY SSKQGGLRRW YNPPWFSEVV 200
    PSTPYDPLVV RNTFEKAVIK RLMTDVPFGV LLSGGLDSSL VASVALRHLE 250
    KSEAACQWGS KLHTFCIGLK GSPDLKAGRE VADYLGTRHH ELHFTVQDGI 300
    DAIEEVIYHV ETYDVTTIRA STPMFLMSRK IKSLGVKMVL SGEGSDEIFG 350
    GYLYFHKAPN KKEFHEETCR KIKALHQYDC LRANKSTSAW GVEARVPFLD 400
    KEFINVAMSI DPEWKMIRPD LGRIEKWVLR NAFDDEKNPY LPKHILYRQK 450
    EQFSDGVGYS WIDGLKDHAN KHVSETMLMN ASFVFPDNTP LTKEAYYYRT 500
    IFEKFFPKSA ARATVPGGPS VACSTAKAVE WDAAWSQNLD PSGRAALGVH 550
    VSAYGEDKTE DSRPEKLQKL AEKTPAIV 578
    Length:578
    Mass (Da):65,227
    Last modified:October 1, 2000 - v1
    Checksum:i2CF8FE216BBDD83E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 831A → D in AAC72836. (PubMed:9881155)Curated
    Sequence conflicti228 – 2281F → L in AAC72836. (PubMed:9881155)Curated
    Sequence conflicti475 – 4751E → D in AAC72836. (PubMed:9881155)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF095452 mRNA. Translation: AAC72836.1.
    AL356332 Genomic DNA. Translation: CAB92065.1.
    AL360334 Genomic DNA. Translation: CAB96680.1.
    CP002688 Genomic DNA. Translation: AED91511.1.
    BT003929 mRNA. Translation: AAO41976.1.
    BT005014 mRNA. Translation: AAO50547.1.
    PIRiT50812.
    T51888.
    RefSeqiNP_196586.1. NM_121062.4. [Q9LFU1-1]
    UniGeneiAt.1637.

    Genome annotation databases

    EnsemblPlantsiAT5G10240.1; AT5G10240.1; AT5G10240. [Q9LFU1-1]
    GeneIDi830888.
    KEGGiath:AT5G10240.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF095452 mRNA. Translation: AAC72836.1 .
    AL356332 Genomic DNA. Translation: CAB92065.1 .
    AL360334 Genomic DNA. Translation: CAB96680.1 .
    CP002688 Genomic DNA. Translation: AED91511.1 .
    BT003929 mRNA. Translation: AAO41976.1 .
    BT005014 mRNA. Translation: AAO50547.1 .
    PIRi T50812.
    T51888.
    RefSeqi NP_196586.1. NM_121062.4. [Q9LFU1-1 ]
    UniGenei At.1637.

    3D structure databases

    ProteinModelPortali Q9LFU1.
    SMRi Q9LFU1. Positions 18-517.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT5G10240.1-P.

    Protein family/group databases

    MEROPSi C44.976.

    Proteomic databases

    PaxDbi Q9LFU1.
    PRIDEi Q9LFU1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G10240.1 ; AT5G10240.1 ; AT5G10240 . [Q9LFU1-1 ]
    GeneIDi 830888.
    KEGGi ath:AT5G10240.

    Organism-specific databases

    TAIRi AT5G10240.

    Phylogenomic databases

    eggNOGi COG0367.
    HOGENOMi HOG000027493.
    InParanoidi Q9LFU1.
    KOi K01953.
    OMAi EKSEAAC.
    PhylomeDBi Q9LFU1.

    Enzyme and pathway databases

    UniPathwayi UPA00134 .
    BioCyci ARA:GQT-424-MONOMER.

    Gene expression databases

    Genevestigatori Q9LFU1.

    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].
    2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(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 nameiASNS3_ARATH
    AccessioniPrimary (citable) accession number: Q9LFU1
    Secondary accession number(s): Q9LEA1, Q9ZST7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2013
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 89 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