ASNS2_ORYSJ
ID ASNS2_ORYSJ Reviewed; 591 AA.
AC Q43011; Q0DD19; Q5Z6P2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
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 OrderedLocusNames=Os06g0265000, LOC_Os06g15420; ORFNames=OJ1001_B06.12;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare; TISSUE=Callus;
RA Sueyoshi K., Kawachi T., Nakajima A., Yamagata H., Sugimoto T., Iwasaki T.,
RA Oji Y.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare; TISSUE=Callus;
RA Watanabe K., Higuchi T., Sakai T., Yamaya T.;
RT "Nucleotide sequence of cDNA encoding asparagine synthetase from rice
RT callus.";
RL (er) Plant Gene Register PGR96-020(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=10965944; DOI=10.1093/pcp/pcd006;
RA Nakano K., Suzuki T., Hayakawa T., Yamaya T.;
RT "Organ and cellular localization of asparagine synthetase in rice plants.";
RL Plant Cell Physiol. 41:874-880(2000).
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; L-
CC asparagine from L-aspartate (L-Gln route): step 1/1.
CC -!- TISSUE SPECIFICITY: Expressed in companion cells of leaf sheath
CC vascular bundles, and phloem-parenchyma cells, nucellar projections and
CC nucellar epidermis of dorsal vascular bundles of grains.
CC {ECO:0000269|PubMed:10965944}.
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DR EMBL; U55873; AAB03991.1; -; mRNA.
DR EMBL; D83378; BAA18951.1; -; mRNA.
DR EMBL; AP005382; BAD54377.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19254.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS97145.1; -; Genomic_DNA.
DR EMBL; CM000143; EEE65484.1; -; Genomic_DNA.
DR EMBL; AK100247; BAG94512.1; -; mRNA.
DR PIR; T03602; T03602.
DR RefSeq; XP_015643183.1; XM_015787697.1.
DR AlphaFoldDB; Q43011; -.
DR SMR; Q43011; -.
DR STRING; 4530.OS06T0265000-01; -.
DR PaxDb; Q43011; -.
DR PRIDE; Q43011; -.
DR EnsemblPlants; Os06t0265000-01; Os06t0265000-01; Os06g0265000.
DR GeneID; 4340706; -.
DR Gramene; Os06t0265000-01; Os06t0265000-01; Os06g0265000.
DR KEGG; osa:4340706; -.
DR eggNOG; KOG0571; Eukaryota.
DR HOGENOM; CLU_014658_2_2_1; -.
DR InParanoid; Q43011; -.
DR OMA; DWSGIYS; -.
DR OrthoDB; 782607at2759; -.
DR BRENDA; 6.3.5.4; 8948.
DR PlantReactome; R-OSA-1119354; Asparagine biosynthesis III.
DR PlantReactome; R-OSA-1119495; Citrulline biosynthesis.
DR PlantReactome; R-OSA-1119553; Asparagine biosynthesis.
DR UniPathway; UPA00134; UER00195.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR ExpressionAtlas; Q43011; baseline and differential.
DR Genevisible; Q43011; OS.
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 Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding;
KW Glutamine amidotransferase; Ligase; Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..591
FT /note="Asparagine synthetase [glutamine-hydrolyzing] 2"
FT /id="PRO_0000056925"
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 591 AA; 66227 MW; 3126C674724E4A3D CRC64;
MCGILAVLGV ADVSLAKRSR IIELSRRLRH RGPDWSGIHC YQDCYLAHQR LAIVDPTSGD
QPLYNEDKSV VVTVNGEIYN HEELKANLKS HKFQTASDCE VIAHLYEEYG EEFVDMLDGM
FAFVLLDTRD KSFIAARDAI GICPLYMGWG LDGSVWFSSE MKALSDDCER FISFPPGHLY
SSKTGGLRRW YNPPWFSESI PSTPYNPLLL RQSFEKAIIK RLMTDVPFGV LLSGGLDSSL
VASVVSRHLA EAKVAAQWGN KLHTFCIGLK GSPDLRAAKE VADYLGTVHH ELHFTVQEGI
DALEEVIYHV ETYDVTTIRA STPMFLMSRK IKSLGVKMVL SGEGSDEIFG GYLYFHKAPN
KKEFHEETCR KIKALHLYDC LRANKSTSAW GVEARVPFLD KNFINVAMDI DPEWKMIKRD
LGRIEKWVLR NAFDDEEKPY LPKHILYRQK EQFSDGVGYS WIDGLKDHAN EHVSDSMMMN
ASFVYPENTP VTKEAYYYRT IFEKFFPKNA ARLTVPGGPS VACSTAKAVE WDAAWSKNLD
PSGRAALGVH DAAYEDTLQK SPASANPVLD NGFGPALGES MVKTVASATA V
