ID   ASNS_SANAU              Reviewed;         525 AA.
AC   O24338;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Asparagine synthetase [glutamine-hydrolyzing];
DE            EC=6.3.5.4;
DE   AltName: Full=Glutamine-dependent asparagine synthetase;
GN   Name=AND1;
OS   Sandersonia aurantiaca (Christmas-bells) (Chinese-lantern lily).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Sandersonia.
OX   NCBI_TaxID=61864;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Tepal;
RA   Eason J.R., King G.A.;
RT   "Nucleotide sequence of cDNA encoding asparagine synthetase from
RT   Sandersonia aurantiaca.";
RL   (er) Plant Gene Register PGR97-112(1997).
CC   -!- FUNCTION: Could play a role in remobilization of nitrogen in flowers
CC       during senescence.
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.
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DR   EMBL; AF005724; AAB71532.1; -; mRNA.
DR   AlphaFoldDB; O24338; -.
DR   SMR; O24338; -.
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   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..525
FT                   /note="Asparagine synthetase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000056928"
FT   DOMAIN          2..185
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   DOMAIN          193..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         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   525 AA;  59609 MW;  5C7471022A11F722 CRC64;
     MCGILAVLGC SDDSQAKRVR VLELSRRLKH RGPDWSGLDH HGDCYLAHQR LAIIDPASGD
     QPLYNEDKTI IVTVNGEIYN HEELRKGLPG HTFRTGSDCE VIAHLYEEHG ESFIHMLDGI
     FSFVLLDSRN NSFVAARDAI GVTPLYIGWG LDGSVWISSE MKGLNDDCEH FKFFPPGHLY
     SSKEGSFKRW YNPPWFSEVI PSVPFDPLAL RKAFEDAVIK RLMTDVPFGV LLSGGLDSSL
     VASVTARYLE GTKAAELWGT QLHSFCVGLE GSPDLKAAKE VANFLGTIHH EFHFTVQDGI
     DAIEDVIYHV ETYDVTTIRA STPMFLMSRK IKSLGVKMVI SGEGSDEIFG GYLYFHKAPN
     KEELHLETCH KIKALHQYDC LRANKATSAW GLEARVPFLD KEFVNVAMSI DPEWKMIKPD
     IGRIEKWILR RAFDDEENPY LPKHILYRQK EQFSDGVGYS WIDGLKAHSA LHVTDKMMLN
     AAHIYPHNTP TTKEAYYYRM IFERFFPQID SPWRSKCGLQ HSKSY