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P49078 (ASNS1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Asparagine synthetase [glutamine-hydrolyzing] 1

EC=6.3.5.4
Alternative name(s):
Glutamine-dependent asparagine synthetase 1
Protein DARK INDUCIBLE 6
Gene names
Name:ASN1
Synonyms:DIN6
Ordered Locus Names:At3g47340
ORF Names:T21L8.90
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length584 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Essential for nitrogen assimilation, distribution and remobilization within the plant via the phloem. Ref.6

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.

Induction

By dark. Down-regulated by light and sucrose. Ref.5

Miscellaneous

Plants over-expressing ASN1 have increased content of free amino acids (mainly Asn) in flowers, siliques and seeds (Ref.6).

Sequence similarities

Contains 1 asparagine synthetase domain.

Contains 1 glutamine amidotransferase type-2 domain.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: P49078-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 584583Asparagine synthetase [glutamine-hydrolyzing] 1
PRO_0000056919

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
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 071910E4C6D02433

FASTA58465,621
        10         20         30         40         50         60 
MCGILAVLGC SDDSQAKRVR VLELSRRLRH RGPDWSGLYQ NGDNYLAHQR LAVIDPASGD 

        70         80         90        100        110        120 
QPLFNEDKTI VVTVNGEIYN HEELRKRLKN HKFRTGSDCE VIAHLYEEYG VDFVDMLDGI 

       130        140        150        160        170        180 
FSFVLLDTRD NSFMVARDAI GVTSLYIGWG LDGSVWISSE MKGLNDDCEH FETFPPGHFY 

       190        200        210        220        230        240 
SSKLGGFKQW YNPPWFNESV PSTPYEPLAI RRAFENAVIK RLMTDVPFGV LLSGGLDSSL 

       250        260        270        280        290        300 
VASITARHLA GTKAAKQWGP QLHSFCVGLE GSPDLKAGKE VAEYLGTVHH EFHFSVQDGI 

       310        320        330        340        350        360 
DAIEDVIYHV ETYDVTTIRA STPMFLMSRK IKSLGVKMVL SGEGADEIFG GYLYFHKAPN 

       370        380        390        400        410        420 
KKEFHQETCR KIKALHKYDC LRANKSTSAF GLEARVPFLD KDFINTAMSL DPESKMIKPE 

       430        440        450        460        470        480 
EGRIEKWVLR RAFDDEERPY LPKHILYRQK EQFSDGVGYS WIDGLKDHAA QNVNDKMMSN 

       490        500        510        520        530        540 
AGHIFPHNTP NTKEAYYYRM IFERFFPQNS ARLTVPGGAT VACSTAKAVE WDASWSNNMD 

       550        560        570        580 
PSGRAAIGVH LSAYDGKNVA LTIPPLKAID NMPMMMGQGV VIQS 

« Hide

References

« Hide 'large scale' references
[1]"Metabolic regulation of the gene encoding glutamine-dependent asparagine synthetase in Arabidopsis thaliana."
Lam H.M., Peng S.S., Coruzzi G.M.
Plant Physiol. 106:1347-1357(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Reciprocal regulation of distinct asparagine synthetase genes by light and metabolites in Arabidopsis thaliana."
Lam H.M., Hsieh M.H., Coruzzi G.
Plant J. 16:345-353(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[6]"Overexpression of the ASN1 gene enhances nitrogen status in seeds of Arabidopsis."
Lam H.M., Wong P., Chan H.K., Yam K.M., Chen L., Chow C.M., Coruzzi G.M.
Plant Physiol. 132:926-935(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L29083 mRNA. Translation: AAA74359.1.
AL096860 Genomic DNA. Translation: CAB51206.1.
CP002686 Genomic DNA. Translation: AEE78264.1.
AF419557 mRNA. Translation: AAL31889.1.
AY072214 mRNA. Translation: AAL60035.1.
AY096592 mRNA. Translation: AAM20242.1.
PIRT12989.
RefSeqNP_190318.1. NM_114602.3. [P49078-1]
UniGeneAt.20782.

3D structure databases

ProteinModelPortalP49078.
SMRP49078. Positions 4-517.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC44.976.

Proteomic databases

PaxDbP49078.
PRIDEP49078.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G47340.1; AT3G47340.1; AT3G47340. [P49078-1]
GeneID823888.
KEGGath:AT3G47340.

Organism-specific databases

TAIRAT3G47340.

Phylogenomic databases

eggNOGCOG0367.
HOGENOMHOG000027493.
InParanoidP49078.
KOK01953.
OMADFINTAM.
PhylomeDBP49078.

Enzyme and pathway databases

BioCycARA:GQT-1413-MONOMER.
ARA:GQT-2583-MONOMER.
UniPathwayUPA00134; UER00195.

Gene expression databases

ArrayExpressP49078.
GenevestigatorP49078.

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 nameASNS1_ARATH
AccessionPrimary (citable) accession number: P49078
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 116 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names