ID   ASNS_ASPOF              Reviewed;         590 AA.
AC   P31752; Q96231;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Asparagine synthetase [glutamine-hydrolyzing];
DE            Short=AS;
DE            EC=6.3.5.4;
OS   Asparagus officinalis (Garden asparagus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asparagaceae;
OC   Asparagoideae; Asparagus.
OX   NCBI_TaxID=4686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Limbras 10; TISSUE=Spear tip;
RX   PubMed=7904077; DOI=10.1104/pp.102.4.1337;
RA   Davies K.M., King G.A.;
RT   "Isolation and characterization of a cDNA clone for a harvest-induced
RT   asparagine synthetase from Asparagus officinalis L.";
RL   Plant Physiol. 102:1337-1340(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Moyle R.L., Davies K.M., King G.A., Farnden K.J.F.;
RT   "Nucleotide sequence of the asparagine synthetase gene from Asparagus
RT   officinalis L.";
RL   (er) Plant Gene Register PGR96-096(1996).
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   -!- DEVELOPMENTAL STAGE: Levels of AS increase markedly after harvest.
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DR   EMBL; X67958; CAA48141.1; -; mRNA.
DR   EMBL; X99552; CAA67889.1; -; Genomic_DNA.
DR   PIR; S25165; S25165.
DR   AlphaFoldDB; P31752; -.
DR   SMR; P31752; -.
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..590
FT                   /note="Asparagine synthetase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000056920"
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"
FT   CONFLICT        513
FT                   /note="F -> L (in Ref. 2; CAA67889)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   590 AA;  66176 MW;  9F7CA48BFE0CA712 CRC64;
     MCGILAVLGC SDDSQAKRVR VLELSRRLKH RGPDWSGLCQ HGDCFLSHQR LAIIDPASGD
     QPLYNEDKSI VVTVNGEIYN HEELRRRLPD HKYRTGSDCE VIAHLYEEHG EDFVDMLDGM
     FSFVLLDTRN NCFVAARDAV GITPLYIGWG LDGSVWLSSE MKGLNDDCEH FEVFPPGNLY
     SSRSGSFRRW YNPQWYNETI PSAPYDPLVL RKAFEDAVIK RLMTDVPFGV LLSGGLDSSL
     VAAVTARHLA GSKAAEQWGT QLHSFCVGLE GSPDLKAAKE VAEYLGTVHH EFHFTVQDGI
     DAIEDVIFHI ETYDVTTIRA STPMFLMARK IKSLGVKMVI SGEGSDEIFG GYLYFHKAPN
     KEEFHHETCR KIKALHQYDC LRANKATSAW GLEARVPFLD KEFMDVAMSI DPESKMIKPD
     LGRIEKWVLR KAFDDEENPY LPKHILYRQK EQFSDGVGYS WIDGLKAHAA KHVTDRMMLN
     AARIYPHNTP TTKEAYYYRM IFERFFPQNS ARFTVPGGPS IACSTAKAIE WDARWSNNLD
     PSGRAALGVH DSAYDPPLPS SISAGKGAAM ITNKKPRIVD VATPGVVIST