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   27-MAR-2024, entry version 145.
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;
GN   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; 39947.Q43011; -.
DR   PaxDb; 39947-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; HYLNFHA; -.
DR   OrthoDB; 684401at2759; -.
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   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; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR01536; asn_synth_AEB; 1.
DR   PANTHER; PTHR11772; ASPARAGINE SYNTHETASE; 1.
DR   PANTHER; PTHR11772:SF2; ASPARAGINE SYNTHETASE [GLUTAMINE-HYDROLYZING]; 1.
DR   Pfam; PF00733; Asn_synthase; 1.
DR   Pfam; PF13537; GATase_7; 1.
DR   PIRSF; PIRSF001589; Asn_synthetase_glu-h; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   Genevisible; Q43011; OS.
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
//