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O24661 (ASNS_TRIVS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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 [glutamine-hydrolyzing]

EC=6.3.5.4
Alternative name(s):
Glutamine-dependent asparagine synthetase
Gene names
Name:AS
OrganismTriphysaria versicolor (Yellow owl's clover)
Taxonomic identifier64093 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsLamialesOrobanchaceaePedicularideaeCastillejinaeTriphysaria

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.

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 [glutamine-hydrolyzing]
PRO_0000056929

Regions

Domain2 – 185184Glutamine amidotransferase type-2
Domain193 – 516324Asparagine synthetase
Nucleotide binding341 – 3422ATP By similarity
Region50 – 545Glutamine binding By similarity
Region75 – 773Glutamine binding By similarity

Sites

Active site21For GATase activity By similarity
Binding site981Glutamine By similarity
Binding site2311ATP; via carbonyl oxygen By similarity
Binding site2671ATP; via amide nitrogen and carbonyl oxygen By similarity
Site3431Important for beta-aspartyl-AMP intermediate formation By similarity

Sequences

Sequence LengthMass (Da)Tools
O24661 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 81D923F9D6BDCCE9

FASTA58665,692
        10         20         30         40         50         60 
MCGILAVLGC SDDSQAKRVR VLELSRRLKH RGPDWSGIHH HGDCYLAHQR LAIVDPASGD 

        70         80         90        100        110        120 
QPLFNEDKRI AVTVNGEIYN HEELRALLPN HKFRTGSDCD VIAHLYEEYG ENFVEMLDGM 

       130        140        150        160        170        180 
FSFVLLDSRD NTFIAARDAF GITSLYIGWG LDGSVWISSE LKGLHDECEN FEVFPPGHVY 

       190        200        210        220        230        240 
SSKTEGFRRW YNPPWFSEAI PSTPYDPLVL RGAFEQAVIK RLMTDVPFGV LLSGGLDSSL 

       250        260        270        280        290        300 
VAAVTARHLA GTKAAKRWGS QLHSFCVGLE GSPDLKAGKE VADYLGTVHH EFLFTVQDGI 

       310        320        330        340        350        360 
DAIEDVIYHI ETYDVTTIRA STPMFLMSRK IKSLGVKMVI SGEGSDEIFG GYLYFHKAPN 

       370        380        390        400        410        420 
KEEFHRETCR KIKALHQYDC LRANKATSAW GLEARVPFLD KEFVNLAMSI DPEAKMIKPD 

       430        440        450        460        470        480 
QGRIEKWILR KAFDDEERPY LPKHILYRQK EQFSDGVGYS WIDGLKAHAE QHVTDKMMLN 

       490        500        510        520        530        540 
AGHIFPHNTP TTKEGYYYRM IFERFFPQNS AKLTVPGGPS VACSTATAVA WDASWSKNLD 

       550        560        570        580 
PSGRAATGVH DLAYENHVPI GNLKSKKMDS VSLGNAVGPQ ELTIRS 

« Hide

References

[1]"Host-root exudates increase gene expression of asparagine synthetase in the roots of a hemiparasitic plant Triphysaria versicolor (Scrophulariaceae)."
Delavault P., Estabrook E., Albrecht H., Wrobel R., Yoder J.I.
Gene 222:155-162(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Root.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF014055 mRNA. Translation: AAD05033.1.
AF014056 mRNA. Translation: AAD05034.1.
AF014057 mRNA. Translation: AAD05035.1.

3D structure databases

ProteinModelPortalO24661.
SMRO24661. Positions 1-517.
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.
InterProIPR006426. Asn_synth_AEB.
IPR001962. Asn_synthase.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
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.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASNS_TRIVS
AccessionPrimary (citable) accession number: O24661
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 75 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