ID   ASNS1_ORYSJ             Reviewed;         604 AA.
AC   Q10MX3; A0A0P0VX10; Q0DSS5;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Asparagine synthetase [glutamine-hydrolyzing] 1;
DE            EC=6.3.5.4;
DE   AltName: Full=Glutamine-dependent asparagine synthetase 1;
GN   OrderedLocusNames=Os03g0291500, LOC_Os03g18130;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RG   The rice full-length cDNA consortium;
RT   "Oryza sativa full length cDNA.";
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAF11713.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC137634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DP000009; ABF95401.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF11713.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014959; BAS83672.1; -; Genomic_DNA.
DR   EMBL; AK318591; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015632089.1; XM_015776603.1.
DR   AlphaFoldDB; Q10MX3; -.
DR   SMR; Q10MX3; -.
DR   STRING; 39947.Q10MX3; -.
DR   PaxDb; 39947-Q10MX3; -.
DR   EnsemblPlants; Os03t0291500-01; Os03t0291500-01; Os03g0291500.
DR   GeneID; 4332506; -.
DR   Gramene; Os03t0291500-01; Os03t0291500-01; Os03g0291500.
DR   KEGG; osa:4332506; -.
DR   eggNOG; KOG0571; Eukaryota.
DR   HOGENOM; CLU_014658_2_2_1; -.
DR   InParanoid; Q10MX3; -.
DR   OMA; FASKHTF; -.
DR   OrthoDB; 367001at2759; -.
DR   BRENDA; 6.3.5.4; 8948.
DR   PlantReactome; R-OSA-1119354; Asparagine biosynthesis III.
DR   PlantReactome; R-OSA-1119553; Asparagine biosynthesis.
DR   UniPathway; UPA00134; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
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:SF16; ASPARAGINE SYNTHETASE [GLUTAMINE-HYDROLYZING] 1; 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; Q10MX3; 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..604
FT                   /note="Asparagine synthetase [glutamine-hydrolyzing] 1"
FT                   /id="PRO_0000420842"
FT   DOMAIN          2..186
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   DOMAIN          211..451
FT                   /note="Asparagine synthetase"
FT   ACT_SITE        2
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
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         99
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         342..343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            344
FT                   /note="Important for beta-aspartyl-AMP intermediate
FT                   formation"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   604 AA;  67322 MW;  029B5770234C20FB CRC64;
     MCGILAVLGA ADWSQAKRAH VLSCSRRLKH RGPDWSGLYQ CEGNFLAQQR LAIVSPLSGD
     QPLYNADRTI VVVANGEIYN HKKIRKQFAS KHTFSTGSDC EVIIPLYEEY GEDFVDMLDG
     VFAFVLYDTR TKTYMAARDA IGVNPLYIGR GSDGAVWISS EMKALNEDCV EFEIFPPGHL
     YSSAAGGLRR WYKPQWFAEN VPATPYQPLL LREAFEKAVI KRLMTDVPFG VLLSGGLDSS
     LVAAVTKRHL IKTEAAEKFG AELHSFVVGL EGSPDLIAAR EVADHLGTIH HEFHFTVQDG
     IDAIEEVIYH DETYDVTTIR ASTPMFLMAR KIKALGVKMV LSGEGSDELL GGYLYFHFAP
     NKEEFHKETC RKVKALHQYD CLRANKATSA WGLEVRVPFL DKEFINVAMS MDPEWKMYNA
     DLGRIEKWVM RKAFDDEEHP YLPKHILYRQ KEQFSDGVGY NWIDGLKAFT EQQVSDEMMK
     NAAKVYPHNT PVNKEAYYYR MIFERLFPQE SARETVPWGP SIACSTPAAI EWVEQWKASH
     DPSGRLIASH NSASASANHT NHANANANGN SNGKANGNCA MAANGTNGVG LVVANGTANG
     KMEA
//