ASNS3_ARATH
ID ASNS3_ARATH Reviewed; 578 AA.
AC Q9LFU1; Q9LEA1; Q9ZST7;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Asparagine synthetase [glutamine-hydrolyzing] 3;
DE EC=6.3.5.4;
DE AltName: Full=Glutamine-dependent asparagine synthetase 3;
GN Name=ASN3; OrderedLocusNames=At5g10240; ORFNames=F18D22.10, T31P16.230;
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].
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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).
CC -!- FUNCTION: Essential for nitrogen assimilation, distribution and
CC remobilization within the plant via the phloem. {ECO:0000250}.
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=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LFU1-1; Sequence=Displayed;
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DR EMBL; AF095452; AAC72836.1; -; mRNA.
DR EMBL; AL356332; CAB92065.1; -; Genomic_DNA.
DR EMBL; AL360334; CAB96680.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91511.1; -; Genomic_DNA.
DR EMBL; BT003929; AAO41976.1; -; mRNA.
DR EMBL; BT005014; AAO50547.1; -; mRNA.
DR PIR; T50812; T50812.
DR PIR; T51888; T51888.
DR RefSeq; NP_196586.1; NM_121062.5. [Q9LFU1-1]
DR AlphaFoldDB; Q9LFU1; -.
DR SMR; Q9LFU1; -.
DR BioGRID; 16166; 2.
DR IntAct; Q9LFU1; 1.
DR STRING; 3702.AT5G10240.1; -.
DR PaxDb; Q9LFU1; -.
DR PRIDE; Q9LFU1; -.
DR ProMEX; Q9LFU1; -.
DR ProteomicsDB; 246863; -. [Q9LFU1-1]
DR EnsemblPlants; AT5G10240.1; AT5G10240.1; AT5G10240. [Q9LFU1-1]
DR GeneID; 830888; -.
DR Gramene; AT5G10240.1; AT5G10240.1; AT5G10240. [Q9LFU1-1]
DR KEGG; ath:AT5G10240; -.
DR Araport; AT5G10240; -.
DR TAIR; locus:2145377; AT5G10240.
DR eggNOG; KOG0571; Eukaryota.
DR HOGENOM; CLU_014658_2_2_1; -.
DR InParanoid; Q9LFU1; -.
DR OMA; HPPAHGE; -.
DR OrthoDB; 782607at2759; -.
DR PhylomeDB; Q9LFU1; -.
DR BRENDA; 6.3.5.4; 399.
DR UniPathway; UPA00134; -.
DR PRO; PR:Q9LFU1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFU1; baseline and differential.
DR Genevisible; Q9LFU1; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0006529; P:asparagine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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] 3"
FT /id="PRO_0000420841"
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 REGION 555..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 CONFLICT 83
FT /note="A -> D (in Ref. 1; AAC72836)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="F -> L (in Ref. 1; AAC72836)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="E -> D (in Ref. 1; AAC72836)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 65227 MW; 2CF8FE216BBDD83E CRC64;
MCGILAVLGC VDNSQAKRSR IIELSRRLRH RGPDWSGLHC YEDCYLAHER LAIVDPTSGD
QPLYNEDKTI AVTVNGEIYN HKALRENLKS HQFRTGSDCE VIAHLYEEHG EEFVDMLDGM
FAFVLLDTRD KSFIAARDAI GITPLYIGWG LDGSVWFASE MKALSDDCEQ FMCFPPGHIY
SSKQGGLRRW YNPPWFSEVV PSTPYDPLVV RNTFEKAVIK RLMTDVPFGV LLSGGLDSSL
VASVALRHLE KSEAACQWGS KLHTFCIGLK GSPDLKAGRE VADYLGTRHH ELHFTVQDGI
DAIEEVIYHV ETYDVTTIRA STPMFLMSRK IKSLGVKMVL SGEGSDEIFG GYLYFHKAPN
KKEFHEETCR KIKALHQYDC LRANKSTSAW GVEARVPFLD KEFINVAMSI DPEWKMIRPD
LGRIEKWVLR NAFDDEKNPY LPKHILYRQK EQFSDGVGYS WIDGLKDHAN KHVSETMLMN
ASFVFPDNTP LTKEAYYYRT IFEKFFPKSA ARATVPGGPS VACSTAKAVE WDAAWSQNLD
PSGRAALGVH VSAYGEDKTE DSRPEKLQKL AEKTPAIV
