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P49093 (ASNS2_LOTJA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. 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] 2

EC=6.3.5.4
Alternative name(s):
Glutamine-dependent asparagine synthetase 2
Gene names
Name:AS2
OrganismLotus japonicus (Lotus corniculatus var. japonicus)
Taxonomic identifier34305 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeLoteaeLotus

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] 2
PRO_0000056923

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
P49093 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8E460FFB526BEF0D

FASTA58665,970
        10         20         30         40         50         60 
MCGILAVLGC SDDSQAKRVR VLELSRRLKH RGPDWSGLHQ HGDNFLAHQR LAIVDPASGD 

        70         80         90        100        110        120 
QPLFNEDQSI IVTVNGEIFN HEELRKQLPN HKFRTGCDCD VIAHLYEEHG ENFVDMLDGI 

       130        140        150        160        170        180 
FSFVLLDTRD NSFLVARDAI GVTSLYIGYG LDGSVWIASE LKGLNDDCEH FELFPPGHLY 

       190        200        210        220        230        240 
SSKEKEFRRW YNPPWFSEAI PSAPYDPLAL RQAFEKAIIK RLMTDVPFGV LLSGGLDSSL 

       250        260        270        280        290        300 
VASVTARYLA DTKAAKQWGS KLHSFCVGLE GAPDLKAARE VADYIGTVHH EFQYTIQDGI 

       310        320        330        340        350        360 
DAIEDVIYHV ETYDVTTIRA GTPMFLMSRK IKSLGVKMVL SGEGSDEIFA GYLYFHKAPN 

       370        380        390        400        410        420 
KEELHQETCS KIKALHKYDC LRANKSTYAW GLEARVPFLD KKFIDVAMGI DPENKMIKRD 

       430        440        450        460        470        480 
EGRIEKWVLR KAFDDEENPY LPKHILYRQK EQFSDGVGYG WIDGLKDHAA KHVTDKMMLN 

       490        500        510        520        530        540 
ASNIYPFNTP NTKEAYYYRM IFERFFPQNS ARLSVPGGAS IACSTEKAIE WDAAWSNNLD 

       550        560        570        580 
PSGRAALGVH DSAYDDQLNK SVSKGVEPEK IIPKMEVSPL GVAILS 

« Hide

References

[1]"Molecular cloning and characterisation of asparagine synthetase from Lotus japonicus: dynamics of asparagine synthesis in N-sufficient conditions."
Waterhouse R.N., Smyth A.J., Massoneau A., Prosser I.M., Clarkson D.T.
Plant Mol. Biol. 30:883-897(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Gifu / B-129.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X89410 mRNA. Translation: CAA61590.1.
PIRS69183.

3D structure databases

ProteinModelPortalP49093.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC44.976.

Proteomic databases

PRIDEP49093.

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.
TIGRFAMsTIGR01536. asn_synth_AEB. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASNS2_LOTJA
AccessionPrimary (citable) accession number: P49093
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 76 of the entry and version 2 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