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P19251 (ASNS1_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Asparagine synthetase, nodule [glutamine-hydrolyzing]

EC=6.3.5.4
Alternative name(s):
Glutamine-dependent asparagine synthetase
Gene names
Name:AS1
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Pathway

Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.

Tissue specificity

Root nodules.

Induction

By darkness.

Sequence similarities

Contains 1 asparagine synthetase domain.

Contains 1 glutamine amidotransferase type-2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 586585Asparagine synthetase, nodule [glutamine-hydrolyzing]
PRO_0000056926

Regions

Domain2 – 185184Glutamine amidotransferase type-2
Domain193 – 517325Asparagine synthetase
Nucleotide binding342 – 3432ATP By similarity
Region50 – 545Glutamine binding By similarity
Region75 – 773Glutamine binding By similarity

Sites

Active site21For GATase activity By similarity
Binding site981Glutamine By similarity
Binding site2321ATP; via carbonyl oxygen By similarity
Binding site2681ATP; via amide nitrogen and carbonyl oxygen By similarity
Site3441Important for beta-aspartyl-AMP intermediate formation By similarity

Sequences

Sequence LengthMass (Da)Tools
P19251 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 17C5019A3C8ED491

FASTA58666,353
        10         20         30         40         50         60 
MCGILAVLGC SDDSQAKRVR ILELSRRLKH RGPDWSGLHQ HGDNYLAHQR LAIVDPASGD 

        70         80         90        100        110        120 
QPLFNEDKSI IVTVNGEIYN HEELRKQLPN HKFFTQCDCD VIAHLYEEHG ENFVDMLDGI 

       130        140        150        160        170        180 
FSFVLLDTRD NSFIVARDAI GVTSLYIGWG LDGSVWIASE LKGLNDECEH FEVFPPGHLY 

       190        200        210        220        230        240 
SSKEREFRRW YNPPWFNEAI IPSTPYDPLV LRNAFEKAVI KRLMTDVPFG VLLSGGLDSS 

       250        260        270        280        290        300 
LVASVTARYL AGTKAAKQWG AKLPSFCVGL KGAPDLKAGK EVADFLGTVH HEFEFTIQDG 

       310        320        330        340        350        360 
IDAIEDVIYH TETYDVTTIR AATPMFLMSR KIKSSGVKWV ISGEGSDEIF GGYLYFHKAP 

       370        380        390        400        410        420 
NREEFHQETC RKIKALHRYD CLRANKSTYA WGLEARVPFL DKDFIKVAMD IDPEFKMIKH 

       430        440        450        460        470        480 
DEGRIEKWIL RKAFDDEENP YLPKHILYRQ KEQFSDGVGY GWIDGIKDHA AKHVTDRMMF 

       490        500        510        520        530        540 
NASHIFPFNT PNTKEAYYYR MIFERFFPQN SARLTVPGGP SVACSTEKAI EWDASWSNNL 

       550        560        570        580 
DPSGRAALGV HVSAYEHQIN PVTKGVEPEK IIPKIGVSPL GVAIQT 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52179 mRNA. Translation: CAA36429.1.
Y13321 Genomic DNA. Translation: CAA73762.1.
PIRAJPMN1. S11444.

3D structure databases

ProteinModelPortalP19251.
SMRP19251. Positions 1-518.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC44.976.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00134; UER00195.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProIPR006426. 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]
PfamPF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view]
PIRSFPIRSF001589. Asn_synthetase_glu-h. 1 hit.
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASNS1_PEA
AccessionPrimary (citable) accession number: P19251
Secondary accession number(s): O49925
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways