ID   ASNS_TRIVS              Reviewed;         586 AA.
AC   O24661;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   22-FEB-2023, entry version 97.
DE   RecName: Full=Asparagine synthetase [glutamine-hydrolyzing];
DE            EC=6.3.5.4;
DE   AltName: Full=Glutamine-dependent asparagine synthetase;
GN   Name=AS;
OS   Triphysaria versicolor (Yellow owl's clover).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Orobanchaceae; Pedicularideae; Castillejinae;
OC   Triphysaria.
OX   NCBI_TaxID=64093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root;
RX   PubMed=9831643; DOI=10.1016/s0378-1119(98)00502-2;
RA   Delavault P., Estabrook E., Albrecht H., Wrobel R., Yoder J.I.;
RT   "Host-root exudates increase gene expression of asparagine synthetase in
RT   the roots of a hemiparasitic plant Triphysaria versicolor
RT   (Scrophulariaceae).";
RL   Gene 222:155-162(1998).
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; AF014055; AAD05033.1; -; mRNA.
DR   EMBL; AF014056; AAD05034.1; -; mRNA.
DR   EMBL; AF014057; AAD05035.1; -; mRNA.
DR   AlphaFoldDB; O24661; -.
DR   SMR; O24661; -.
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; 3.60.20.10; 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   PANTHER; PTHR11772; ASPARAGINE SYNTHETASE; 1.
DR   PANTHER; PTHR11772:SF48; 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.
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_0000056929"
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   586 AA;  65692 MW;  81D923F9D6BDCCE9 CRC64;
     MCGILAVLGC SDDSQAKRVR VLELSRRLKH RGPDWSGIHH HGDCYLAHQR LAIVDPASGD
     QPLFNEDKRI AVTVNGEIYN HEELRALLPN HKFRTGSDCD VIAHLYEEYG ENFVEMLDGM
     FSFVLLDSRD NTFIAARDAF GITSLYIGWG LDGSVWISSE LKGLHDECEN FEVFPPGHVY
     SSKTEGFRRW YNPPWFSEAI PSTPYDPLVL RGAFEQAVIK RLMTDVPFGV LLSGGLDSSL
     VAAVTARHLA GTKAAKRWGS QLHSFCVGLE GSPDLKAGKE VADYLGTVHH EFLFTVQDGI
     DAIEDVIYHI ETYDVTTIRA STPMFLMSRK IKSLGVKMVI SGEGSDEIFG GYLYFHKAPN
     KEEFHRETCR KIKALHQYDC LRANKATSAW GLEARVPFLD KEFVNLAMSI DPEAKMIKPD
     QGRIEKWILR KAFDDEERPY LPKHILYRQK EQFSDGVGYS WIDGLKAHAE QHVTDKMMLN
     AGHIFPHNTP TTKEGYYYRM IFERFFPQNS AKLTVPGGPS VACSTATAVA WDASWSKNLD
     PSGRAATGVH DLAYENHVPI GNLKSKKMDS VSLGNAVGPQ ELTIRS
//