ASNS1_ARATH
ID ASNS1_ARATH Reviewed; 584 AA.
AC P49078;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Asparagine synthetase [glutamine-hydrolyzing] 1;
DE EC=6.3.5.4;
DE AltName: Full=Glutamine-dependent asparagine synthetase 1;
DE AltName: Full=Protein DARK INDUCIBLE 6;
GN Name=ASN1; Synonyms=DIN6; OrderedLocusNames=At3g47340; ORFNames=T21L8.90;
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].
RC STRAIN=cv. Columbia;
RX PubMed=7846154; DOI=10.1104/pp.106.4.1347;
RA Lam H.M., Peng S.S., Coruzzi G.M.;
RT "Metabolic regulation of the gene encoding glutamine-dependent asparagine
RT synthetase in Arabidopsis thaliana.";
RL Plant Physiol. 106:1347-1357(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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 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 [6]
RP FUNCTION.
RX PubMed=12805621; DOI=10.1104/pp.103.020123;
RA Lam H.M., Wong P., Chan H.K., Yam K.M., Chen L., Chow C.M., Coruzzi G.M.;
RT "Overexpression of the ASN1 gene enhances nitrogen status in seeds of
RT Arabidopsis.";
RL Plant Physiol. 132:926-935(2003).
CC -!- FUNCTION: Essential for nitrogen assimilation, distribution and
CC remobilization within the plant via the phloem.
CC {ECO:0000269|PubMed:12805621}.
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; L-
CC asparagine from L-aspartate (L-Gln route): step 1/1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P49078-1; Sequence=Displayed;
CC -!- INDUCTION: By dark. Down-regulated by light and sucrose.
CC {ECO:0000269|PubMed:9881155}.
CC -!- MISCELLANEOUS: Plants over-expressing ASN1 have increased content of
CC free amino acids (mainly Asn) in flowers, siliques and seeds.
CC {ECO:0000305|PubMed:12805621}.
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DR EMBL; L29083; AAA74359.1; -; mRNA.
DR EMBL; AL096860; CAB51206.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78264.1; -; Genomic_DNA.
DR EMBL; AF419557; AAL31889.1; -; mRNA.
DR EMBL; AY072214; AAL60035.1; -; mRNA.
DR EMBL; AY096592; AAM20242.1; -; mRNA.
DR PIR; T12989; T12989.
DR RefSeq; NP_190318.1; NM_114602.4. [P49078-1]
DR AlphaFoldDB; P49078; -.
DR SMR; P49078; -.
DR STRING; 3702.AT3G47340.1; -.
DR PaxDb; P49078; -.
DR PRIDE; P49078; -.
DR ProteomicsDB; 246521; -. [P49078-1]
DR EnsemblPlants; AT3G47340.1; AT3G47340.1; AT3G47340. [P49078-1]
DR GeneID; 823888; -.
DR Gramene; AT3G47340.1; AT3G47340.1; AT3G47340. [P49078-1]
DR KEGG; ath:AT3G47340; -.
DR Araport; AT3G47340; -.
DR TAIR; locus:2099580; AT3G47340.
DR eggNOG; KOG0571; Eukaryota.
DR InParanoid; P49078; -.
DR PhylomeDB; P49078; -.
DR UniPathway; UPA00134; UER00195.
DR PRO; PR:P49078; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P49078; baseline and differential.
DR Genevisible; P49078; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; ISS:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006529; P:asparagine biosynthetic process; IGI:UniProtKB.
DR GO; GO:0009063; P:cellular amino acid catabolic process; TAS:TAIR.
DR GO; GO:0043617; P:cellular response to sucrose starvation; IEP:TAIR.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009646; P:response to absence of light; TAS:TAIR.
DR GO; GO:0009750; P:response to fructose; IEP:TAIR.
DR GO; GO:0009749; P:response to glucose; IEP:TAIR.
DR GO; GO:0009744; P:response to sucrose; IEP:TAIR.
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..584
FT /note="Asparagine synthetase [glutamine-hydrolyzing] 1"
FT /id="PRO_0000056919"
FT DOMAIN 2..185
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 193..516
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"
SQ SEQUENCE 584 AA; 65621 MW; 071910E4C6D02433 CRC64;
MCGILAVLGC SDDSQAKRVR VLELSRRLRH RGPDWSGLYQ NGDNYLAHQR LAVIDPASGD
QPLFNEDKTI VVTVNGEIYN HEELRKRLKN HKFRTGSDCE VIAHLYEEYG VDFVDMLDGI
FSFVLLDTRD NSFMVARDAI GVTSLYIGWG LDGSVWISSE MKGLNDDCEH FETFPPGHFY
SSKLGGFKQW YNPPWFNESV PSTPYEPLAI RRAFENAVIK RLMTDVPFGV LLSGGLDSSL
VASITARHLA GTKAAKQWGP QLHSFCVGLE GSPDLKAGKE VAEYLGTVHH EFHFSVQDGI
DAIEDVIYHV ETYDVTTIRA STPMFLMSRK IKSLGVKMVL SGEGADEIFG GYLYFHKAPN
KKEFHQETCR KIKALHKYDC LRANKSTSAF GLEARVPFLD KDFINTAMSL DPESKMIKPE
EGRIEKWVLR RAFDDEERPY LPKHILYRQK EQFSDGVGYS WIDGLKDHAA QNVNDKMMSN
AGHIFPHNTP NTKEAYYYRM IFERFFPQNS ARLTVPGGAT VACSTAKAVE WDASWSNNMD
PSGRAAIGVH LSAYDGKNVA LTIPPLKAID NMPMMMGQGV VIQS
