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Q9LFU1 (ASNS3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. 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] 3

EC=6.3.5.4
Alternative name(s):
Glutamine-dependent asparagine synthetase 3
Gene names
Name:ASN3
Ordered Locus Names:At5g10240
ORF Names:F18D22.10, T31P16.230
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length578 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 By similarity.

Catalytic activity

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

Pathway

Amino-acid biosynthesis; L-asparagine biosynthesis.

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: Q9LFU1-1)

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 – 578577Asparagine synthetase [glutamine-hydrolyzing] 3
PRO_0000420841

Regions

Domain2 – 185184Glutamine amidotransferase type-2
Domain210 – 450241Asparagine 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 conflict831A → D in AAC72836. Ref.1
Sequence conflict2281F → L in AAC72836. Ref.1
Sequence conflict4751E → D in AAC72836. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 2CF8FE216BBDD83E

FASTA57865,227
        10         20         30         40         50         60 
MCGILAVLGC VDNSQAKRSR IIELSRRLRH RGPDWSGLHC YEDCYLAHER LAIVDPTSGD 

        70         80         90        100        110        120 
QPLYNEDKTI AVTVNGEIYN HKALRENLKS HQFRTGSDCE VIAHLYEEHG EEFVDMLDGM 

       130        140        150        160        170        180 
FAFVLLDTRD KSFIAARDAI GITPLYIGWG LDGSVWFASE MKALSDDCEQ FMCFPPGHIY 

       190        200        210        220        230        240 
SSKQGGLRRW YNPPWFSEVV PSTPYDPLVV RNTFEKAVIK RLMTDVPFGV LLSGGLDSSL 

       250        260        270        280        290        300 
VASVALRHLE KSEAACQWGS KLHTFCIGLK GSPDLKAGRE VADYLGTRHH ELHFTVQDGI 

       310        320        330        340        350        360 
DAIEEVIYHV ETYDVTTIRA STPMFLMSRK IKSLGVKMVL SGEGSDEIFG GYLYFHKAPN 

       370        380        390        400        410        420 
KKEFHEETCR KIKALHQYDC LRANKSTSAW GVEARVPFLD KEFINVAMSI DPEWKMIRPD 

       430        440        450        460        470        480 
LGRIEKWVLR NAFDDEKNPY LPKHILYRQK EQFSDGVGYS WIDGLKDHAN KHVSETMLMN 

       490        500        510        520        530        540 
ASFVFPDNTP LTKEAYYYRT IFEKFFPKSA ARATVPGGPS VACSTAKAVE WDAAWSQNLD 

       550        560        570 
PSGRAALGVH VSAYGEDKTE DSRPEKLQKL AEKTPAIV 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF095452 mRNA. Translation: AAC72836.1.
AL356332 Genomic DNA. Translation: CAB92065.1.
AL360334 Genomic DNA. Translation: CAB96680.1.
CP002688 Genomic DNA. Translation: AED91511.1.
BT003929 mRNA. Translation: AAO41976.1.
BT005014 mRNA. Translation: AAO50547.1.
PIRT50812.
T51888.
RefSeqNP_196586.1. NM_121062.4. [Q9LFU1-1]
UniGeneAt.1637.

3D structure databases

ProteinModelPortalQ9LFU1.
SMRQ9LFU1. Positions 18-517.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT5G10240.1-P.

Protein family/group databases

MEROPSC44.976.

Proteomic databases

PaxDbQ9LFU1.
PRIDEQ9LFU1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G10240.1; AT5G10240.1; AT5G10240. [Q9LFU1-1]
GeneID830888.
KEGGath:AT5G10240.

Organism-specific databases

TAIRAT5G10240.

Phylogenomic databases

eggNOGCOG0367.
HOGENOMHOG000027493.
InParanoidQ9LFU1.
KOK01953.
OMAEKSEAAC.
PhylomeDBQ9LFU1.

Enzyme and pathway databases

BioCycARA:GQT-424-MONOMER.
UniPathwayUPA00134.

Gene expression databases

GenevestigatorQ9LFU1.

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 nameASNS3_ARATH
AccessionPrimary (citable) accession number: Q9LFU1
Secondary accession number(s): Q9LEA1, Q9ZST7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2013
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 88 of the entry and version 1 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