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P31752 (ASNS_ASPOF) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. 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]

Short name=AS
EC=6.3.5.4
OrganismAsparagus officinalis (Garden asparagus)
Taxonomic identifier4686 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAsparagalesAsparagaceaeAsparagoideaeAsparagus

Protein attributes

Sequence length590 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.

Developmental stage

Levels of AS increase markedly after harvest.

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 – 590589Asparagine synthetase [glutamine-hydrolyzing]
PRO_0000056920

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

Experimental info

Sequence conflict5131F → L in CAA67889. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P31752 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9F7CA48BFE0CA712

FASTA59066,176
        10         20         30         40         50         60 
MCGILAVLGC SDDSQAKRVR VLELSRRLKH RGPDWSGLCQ HGDCFLSHQR LAIIDPASGD 

        70         80         90        100        110        120 
QPLYNEDKSI VVTVNGEIYN HEELRRRLPD HKYRTGSDCE VIAHLYEEHG EDFVDMLDGM 

       130        140        150        160        170        180 
FSFVLLDTRN NCFVAARDAV GITPLYIGWG LDGSVWLSSE MKGLNDDCEH FEVFPPGNLY 

       190        200        210        220        230        240 
SSRSGSFRRW YNPQWYNETI PSAPYDPLVL RKAFEDAVIK RLMTDVPFGV LLSGGLDSSL 

       250        260        270        280        290        300 
VAAVTARHLA GSKAAEQWGT QLHSFCVGLE GSPDLKAAKE VAEYLGTVHH EFHFTVQDGI 

       310        320        330        340        350        360 
DAIEDVIFHI ETYDVTTIRA STPMFLMARK IKSLGVKMVI SGEGSDEIFG GYLYFHKAPN 

       370        380        390        400        410        420 
KEEFHHETCR KIKALHQYDC LRANKATSAW GLEARVPFLD KEFMDVAMSI DPESKMIKPD 

       430        440        450        460        470        480 
LGRIEKWVLR KAFDDEENPY LPKHILYRQK EQFSDGVGYS WIDGLKAHAA KHVTDRMMLN 

       490        500        510        520        530        540 
AARIYPHNTP TTKEAYYYRM IFERFFPQNS ARFTVPGGPS IACSTAKAIE WDARWSNNLD 

       550        560        570        580        590 
PSGRAALGVH DSAYDPPLPS SISAGKGAAM ITNKKPRIVD VATPGVVIST 

« Hide

References

[1]"Isolation and characterization of a cDNA clone for a harvest-induced asparagine synthetase from Asparagus officinalis L."
Davies K.M., King G.A.
Plant Physiol. 102:1337-1340(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Limbras 10.
Tissue: Spear tip.
[2]"Nucleotide sequence of the asparagine synthetase gene from Asparagus officinalis L."
Moyle R.L., Davies K.M., King G.A., Farnden K.J.F.
Plant Gene Register PGR96-096
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X67958 mRNA. Translation: CAA48141.1.
X99552 Genomic DNA. Translation: CAA67889.1.
PIRS25165.

3D structure databases

ProteinModelPortalP31752.
SMRP31752. Positions 1-517.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC44.976.

Proteomic databases

PRIDEP31752.

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

Entry information

Entry nameASNS_ASPOF
AccessionPrimary (citable) accession number: P31752
Secondary accession number(s): Q96231
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 81 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