ASNS2_ARATH
ID ASNS2_ARATH Reviewed; 578 AA.
AC Q9LV77; F4KGG8; Q9ZST6;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Asparagine synthetase [glutamine-hydrolyzing] 2;
DE EC=6.3.5.4;
DE AltName: Full=Glutamine-dependent asparagine synthetase 2;
GN Name=ASN2; OrderedLocusNames=At5g65010; ORFNames=MXK3.25;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9881155; DOI=10.1046/j.1365-313x.1998.00302.x;
RA Lam H.M., Hsieh M.H., Coruzzi G.;
RT "Reciprocal regulation of distinct asparagine synthetase genes by light and
RT metabolites in Arabidopsis thaliana.";
RL Plant J. 16:345-353(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP INDUCTION.
RX PubMed=14671018; DOI=10.1104/pp.103.033126;
RA Wong H.K., Chan H.K., Coruzzi G.M., Lam H.M.;
RT "Correlation of ASN2 gene expression with ammonium metabolism in
RT Arabidopsis.";
RL Plant Physiol. 134:332-338(2004).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=21478030; DOI=10.1016/j.plaphy.2011.03.010;
RA Maaroufi-Dguimi H., Debouba M., Gaufichon L., Clement G., Gouia H.,
RA Hajjaji A., Suzuki A.;
RT "An Arabidopsis mutant disrupted in ASN2 encoding asparagine synthetase 2
RT exhibits low salt stress tolerance.";
RL Plant Physiol. Biochem. 49:623-628(2011).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22789031; DOI=10.1111/j.1365-3040.2012.02576.x;
RA Gaufichon L., Masclaux-Daubresse C., Tcherkez G., Reisdorf-Cren M.,
RA Sakakibara Y., Hase T., Clement G., Avice J.C., Grandjean O., Marmagne A.,
RA Boutet-Mercey S., Azzopardi M., Soulay F., Suzuki A.;
RT "Arabidopsis thaliana ASN2 encoding asparagine synthetase is involved in
RT the control of nitrogen assimilation and export during vegetative growth.";
RL Plant Cell Environ. 36:328-342(2013).
CC -!- FUNCTION: Essential for nitrogen assimilation, distribution and
CC remobilization within the plant via the phloem.
CC {ECO:0000269|PubMed:22789031}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate +
CC H(+) + L-asparagine + L-glutamate; Xref=Rhea:RHEA:12228,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58048, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.4;
CC -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LV77-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LV77-2; Sequence=VSP_044714;
CC -!- TISSUE SPECIFICITY: Expressed in the vascular region adjacent to leaf
CC mesophyll cells in the companion cell-sieve tube element complex.
CC {ECO:0000269|PubMed:22789031, ECO:0000269|PubMed:9881155}.
CC -!- INDUCTION: By light and sucrose. Down-regulated by dark.
CC {ECO:0000269|PubMed:14671018, ECO:0000269|PubMed:22789031,
CC ECO:0000269|PubMed:9881155}.
CC -!- DISRUPTION PHENOTYPE: Pale green leaf phenotype and reduction of
CC biomass in mature plants. Increased levels of asparagine, proline and
CC ammonium in response to salt treatment. {ECO:0000269|PubMed:21478030,
CC ECO:0000269|PubMed:22789031}.
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DR EMBL; AF095453; AAC72837.1; -; mRNA.
DR EMBL; AB019236; BAA97313.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97984.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97985.1; -; Genomic_DNA.
DR EMBL; AF367340; AAK32927.1; -; mRNA.
DR EMBL; AY124866; AAM70575.1; -; mRNA.
DR RefSeq; NP_201306.2; NM_125900.2. [Q9LV77-2]
DR RefSeq; NP_851272.1; NM_180941.3. [Q9LV77-1]
DR AlphaFoldDB; Q9LV77; -.
DR SMR; Q9LV77; -.
DR STRING; 3702.AT5G65010.2; -.
DR iPTMnet; Q9LV77; -.
DR PaxDb; Q9LV77; -.
DR PRIDE; Q9LV77; -.
DR ProMEX; Q9LV77; -.
DR ProteomicsDB; 246862; -. [Q9LV77-1]
DR EnsemblPlants; AT5G65010.1; AT5G65010.1; AT5G65010. [Q9LV77-1]
DR EnsemblPlants; AT5G65010.2; AT5G65010.2; AT5G65010. [Q9LV77-2]
DR GeneID; 836625; -.
DR Gramene; AT5G65010.1; AT5G65010.1; AT5G65010. [Q9LV77-1]
DR Gramene; AT5G65010.2; AT5G65010.2; AT5G65010. [Q9LV77-2]
DR KEGG; ath:AT5G65010; -.
DR Araport; AT5G65010; -.
DR TAIR; locus:2177694; AT5G65010.
DR eggNOG; KOG0571; Eukaryota.
DR HOGENOM; CLU_014658_2_2_1; -.
DR InParanoid; Q9LV77; -.
DR OMA; DWSGIYS; -.
DR OrthoDB; 782607at2759; -.
DR PhylomeDB; Q9LV77; -.
DR UniPathway; UPA00134; -.
DR PRO; PR:Q9LV77; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LV77; baseline and differential.
DR Genevisible; Q9LV77; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0097164; P:ammonium ion metabolic process; IMP:TAIR.
DR GO; GO:0006529; P:asparagine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01991; Asn_Synthase_B_C; 1.
DR CDD; cd00712; AsnB; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR006426; Asn_synth_AEB.
DR InterPro; IPR001962; Asn_synthase.
DR InterPro; IPR033738; AsnB_N.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00733; Asn_synthase; 1.
DR Pfam; PF13537; GATase_7; 1.
DR PIRSF; PIRSF001589; Asn_synthetase_glu-h; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01536; asn_synth_AEB; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Amino-acid biosynthesis; Asparagine biosynthesis;
KW ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..578
FT /note="Asparagine synthetase [glutamine-hydrolyzing] 2"
FT /id="PRO_0000420840"
FT DOMAIN 2..185
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 210..450
FT /note="Asparagine synthetase"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 50..54
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250"
FT BINDING 75..77
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 341..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 343
FT /note="Important for beta-aspartyl-AMP intermediate
FT formation"
FT /evidence="ECO:0000250"
FT VAR_SEQ 508
FT /note="K -> KQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044714"
FT CONFLICT 484
FT /note="V -> F (in Ref. 1; AAC72837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 65030 MW; CAEAD8DC90F3A773 CRC64;
MCGILAVLGC IDNSQAKRSR IIELSRRLRH RGPDWSGLHC YEDCYLAHER LAIIDPTSGD
QPLYNEDKTV AVTVNGEIYN HKILREKLKS HQFRTGSDCE VIAHLYEEHG EEFIDMLDGM
FAFVLLDTRD KSFIAARDAI GITPLYIGWG LDGSVWFASE MKALSDDCEQ FMSFPPGHIY
SSKQGGLRRW YNPPWYNEQV PSTPYDPLVL RNAFEKAVIK RLMTDVPFGV LLSGGLDSSL
VAAVALRHLE KSEAARQWGS QLHTFCIGLQ GSPDLKAGRE VADYLGTRHH EFQFTVQDGI
DAIEEVIYHI ETYDVTTIRA STPMFLMSRK IKSLGVKMVL SGEGSDEILG GYLYFHKAPN
KKEFHEETCR KIKALHQFDC LRANKSTSAW GVEARVPFLD KEFLNVAMSI DPEWKLIKPD
LGRIEKWVLR NAFDDEERPY LPKHILYRQK EQFSDGVGYS WIDGLKDHAN KHVSDTMLSN
ASFVFPDNTP LTKEAYYYRT IFEKFFPKSA ARATVPGGPS IACSTAKAVE WDATWSKNLD
PSGRAALGVH VAAYEEDKAA AAAKAGSDLV DPLPKNGT
