ID   ASNS_BRAOL              Reviewed;         586 AA.
AC   P49091;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Asparagine synthetase [glutamine-hydrolyzing];
DE            EC=6.3.5.4;
DE   AltName: Full=Glutamine-dependent asparagine synthetase;
OS   Brassica oleracea (Wild cabbage).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3712;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Shogun;
RA   Downs C.G., Pogson B.J., Davies K.M., Almira E.C.;
RT   "An asparagine synthetase cDNA clone from Broccoli (Brassica oleracea
RT   L.).";
RL   (er) Plant Gene Register PGR95-016(1995).
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   -!- SIMILARITY: Belongs to the asparagine synthetase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X84448; CAA59138.1; -; mRNA.
DR   PIR; S52387; S52387.
DR   AlphaFoldDB; P49091; -.
DR   SMR; P49091; -.
DR   UniPathway; UPA00134; UER00195.
DR   GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..586
FT                   /note="Asparagine synthetase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000056921"
FT   DOMAIN          2..185
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   DOMAIN          194..517
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         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   586 AA;  65673 MW;  DC58CDE0DF3EF4BA CRC64;
     MCGILAVLGC SDDSQAKRVR VLELSRRLRH RGPDWSGIYQ NGFNYLAHQR LAIIDPDSGD
     QPLFNEDKSI VVTVNGEIYN HEELRKGLKN HKFHTGSDCD VIAHLYEEHG ENFVDMLDGI
     FSFVLLDTRD NSFMVARDAV GVTSLYIGWG LDGSLWVSSE MKGLHEDCEH FEAFPPGHLY
     SSKSGGGFKQ WYNPPWFNES VPSTPYEPLA IRSAFEDAVI KRLMTDVPFG VLLSGGLDSS
     LVASITARHL AGTKAAKRWG PQLHSFCVGL EGSPDLKAGK EVAEYLGTVH HEFHFTVQDG
     IDAIEDVIYH VETYDVTTIR ASTPMFLMSR KIKSLGVKMV LSGEGSDEIF GGYLYFHKAP
     NKQEFHQETC RKIKALHKYD CLRANKATSA FGLEARVPFL DKEFINTAMS LDPESKMIKP
     EEGRIEKWVL RRAFDDEERP YLPKHILYRQ KEQFSDGVGY SWIDGLKAHA AENVNDKMMS
     KAAFIFPHNT PLTKEAYYYR MIFERFFPQN SARLTVPGGA TVACSTAKAV EWDASWSNNM
     DPSGRAAIGV HLSAYDGSKV ALPLPAPHKA IDDIPMMMGQ EVVIQT