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P19251

- ASNS1_PEA

UniProt

P19251 - ASNS1_PEA

Protein

Asparagine synthetase, nodule [glutamine-hydrolyzing]

Gene

AS1

Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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 sitei232 – 2321ATP; via carbonyl oxygenBy similarity
    Binding sitei268 – 2681ATP; via amide nitrogen and carbonyl oxygenBy similarity
    Sitei344 – 3441Important for beta-aspartyl-AMP intermediate formationBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi342 – 3432ATPBy 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

    UniPathwayiUPA00134; UER00195.

    Protein family/group databases

    MEROPSiC44.976.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Asparagine synthetase, nodule [glutamine-hydrolyzing] (EC:6.3.5.4)
    Alternative name(s):
    Glutamine-dependent asparagine synthetase
    Gene namesi
    Name:AS1
    OrganismiPisum sativum (Garden pea)
    Taxonomic identifieri3888 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 586585Asparagine synthetase, nodule [glutamine-hydrolyzing]PRO_0000056926Add
    BLAST

    Expressioni

    Tissue specificityi

    Root nodules.

    Inductioni

    By darkness.

    Structurei

    3D structure databases

    ProteinModelPortaliP19251.
    SMRiP19251. Positions 1-518.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 185184Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
    BLAST
    Domaini193 – 517325Asparagine 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

    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.
    PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P19251-1 [UniParc]FASTAAdd to Basket

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    MCGILAVLGC SDDSQAKRVR ILELSRRLKH RGPDWSGLHQ HGDNYLAHQR    50
    LAIVDPASGD QPLFNEDKSI IVTVNGEIYN HEELRKQLPN HKFFTQCDCD 100
    VIAHLYEEHG ENFVDMLDGI FSFVLLDTRD NSFIVARDAI GVTSLYIGWG 150
    LDGSVWIASE LKGLNDECEH FEVFPPGHLY SSKEREFRRW YNPPWFNEAI 200
    IPSTPYDPLV LRNAFEKAVI KRLMTDVPFG VLLSGGLDSS LVASVTARYL 250
    AGTKAAKQWG AKLPSFCVGL KGAPDLKAGK EVADFLGTVH HEFEFTIQDG 300
    IDAIEDVIYH TETYDVTTIR AATPMFLMSR KIKSSGVKWV ISGEGSDEIF 350
    GGYLYFHKAP NREEFHQETC RKIKALHRYD CLRANKSTYA WGLEARVPFL 400
    DKDFIKVAMD IDPEFKMIKH DEGRIEKWIL RKAFDDEENP YLPKHILYRQ 450
    KEQFSDGVGY GWIDGIKDHA AKHVTDRMMF NASHIFPFNT PNTKEAYYYR 500
    MIFERFFPQN SARLTVPGGP SVACSTEKAI EWDASWSNNL DPSGRAALGV 550
    HVSAYEHQIN PVTKGVEPEK IIPKIGVSPL GVAIQT 586
    Length:586
    Mass (Da):66,353
    Last modified:January 23, 2007 - v3
    Checksum:i17C5019A3C8ED491
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52179 mRNA. Translation: CAA36429.1.
    Y13321 Genomic DNA. Translation: CAA73762.1.
    PIRiS11444. AJPMN1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52179 mRNA. Translation: CAA36429.1 .
    Y13321 Genomic DNA. Translation: CAA73762.1 .
    PIRi S11444. AJPMN1.

    3D structure databases

    ProteinModelPortali P19251.
    SMRi P19251. Positions 1-518.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C44.976.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00134 ; UER00195 .

    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.
    PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Dark-induced and organ-specific expression of two asparagine synthetase genes in Pisum sativum."
      Tsai F.Y., Coruzzi G.M.
      EMBO J. 9:323-332(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Sparkle.
      Tissue: Root nodule.
    2. "Light-induced transcriptional repression of the pea AS1 gene: identification of cis-elements and transfactors."
      Ngai N., Tsai F.Y., Coruzzi G.M.
      Plant J. 12:1021-1034(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 1-84.
      Strain: cv. Feltham First.

    Entry informationi

    Entry nameiASNS1_PEA
    AccessioniPrimary (citable) accession number: P19251
    Secondary accession number(s): O49925
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 86 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3