ID   ASNS2_LOTJA             Reviewed;         586 AA.
AC   P49093;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Asparagine synthetase [glutamine-hydrolyzing] 2;
DE            EC=6.3.5.4;
DE   AltName: Full=Glutamine-dependent asparagine synthetase 2;
GN   Name=AS2;
OS   Lotus japonicus (Lotus corniculatus var. japonicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Gifu / B-129;
RX   PubMed=8639748; DOI=10.1007/bf00020801;
RA   Waterhouse R.N., Smyth A.J., Massoneau A., Prosser I.M., Clarkson D.T.;
RT   "Molecular cloning and characterisation of asparagine synthetase from Lotus
RT   japonicus: dynamics of asparagine synthesis in N-sufficient conditions.";
RL   Plant Mol. Biol. 30:883-897(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.
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DR   EMBL; X89410; CAA61590.1; -; mRNA.
DR   PIR; S69183; S69183.
DR   AlphaFoldDB; P49093; -.
DR   SMR; P49093; -.
DR   PRIDE; P49093; -.
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] 2"
FT                   /id="PRO_0000056923"
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;  65970 MW;  8E460FFB526BEF0D CRC64;
     MCGILAVLGC SDDSQAKRVR VLELSRRLKH RGPDWSGLHQ HGDNFLAHQR LAIVDPASGD
     QPLFNEDQSI IVTVNGEIFN HEELRKQLPN HKFRTGCDCD VIAHLYEEHG ENFVDMLDGI
     FSFVLLDTRD NSFLVARDAI GVTSLYIGYG LDGSVWIASE LKGLNDDCEH FELFPPGHLY
     SSKEKEFRRW YNPPWFSEAI PSAPYDPLAL RQAFEKAIIK RLMTDVPFGV LLSGGLDSSL
     VASVTARYLA DTKAAKQWGS KLHSFCVGLE GAPDLKAARE VADYIGTVHH EFQYTIQDGI
     DAIEDVIYHV ETYDVTTIRA GTPMFLMSRK IKSLGVKMVL SGEGSDEIFA GYLYFHKAPN
     KEELHQETCS KIKALHKYDC LRANKSTYAW GLEARVPFLD KKFIDVAMGI DPENKMIKRD
     EGRIEKWVLR KAFDDEENPY LPKHILYRQK EQFSDGVGYG WIDGLKDHAA KHVTDKMMLN
     ASNIYPFNTP NTKEAYYYRM IFERFFPQNS ARLSVPGGAS IACSTEKAIE WDAAWSNNLD
     PSGRAALGVH DSAYDDQLNK SVSKGVEPEK IIPKMEVSPL GVAILS