ID   ASNS1_LOTJA             Reviewed;         586 AA.
AC   P49092;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Asparagine synthetase [glutamine-hydrolyzing] 1;
DE            EC=6.3.5.4;
DE   AltName: Full=Glutamine-dependent asparagine synthetase 1;
GN   Name=AS1;
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.
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; X89409; CAA61589.1; -; mRNA.
DR   PIR; S69182; S69182.
DR   AlphaFoldDB; P49092; -.
DR   SMR; P49092; -.
DR   ProMEX; P49092; -.
DR   OMA; LFGYKYT; -.
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] 1"
FT                   /id="PRO_0000056922"
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;  66461 MW;  AD32149B6A70CEEE CRC64;
     MCGILAVLGC SDFTQAKRVR VLELSRRLKH RGPDWSGLHQ HGDCYLAHQR LAIVDPASGD
     QPLFNEDKSI IVTVNGEIYN HEELRKQLPN HQFRTGSDCD VIAHLYEEHG ENFMDMLDGI
     FSFVLLDTRD NTFIVARDAI GVTSLYIGWG LDGSVWISSE MKGLNDDCEH FEVFPPGHLY
     SSRERAFRRW YNPTWFSESI PSAPYDPLAV RHAFEKAVIK RLMTDVPFGV LLSGGLDSSL
     VASITSRYLA TTKAAEQWGS KLHSFCVGLE GSPDLKAAKE VADYLGTVHH EFTFTVQDGI
     DAIEEVIYHV ETYDVTTIRA STPMFLMSRK IKSLGVKWVI SGEGSDEIFG GYLYFHKAPN
     KEEFHTETCR KIKALHQYDC LRANKSTFAW GLEARVPFLD KEFINVAMNI DPEYKMIKRD
     EGRIEKYILR RAFDDEEKPY LPKHILYRQK EQFSDGVGYS WIDGLKDHAA KHVTDKMILN
     AGNIFRHNTP LTKEAYYYRM IFERFFPQNS ARLTVPGGPT VACSTAKAVE WDAAWSNNLD
     PSGRAALGVH LSAYDDKQNN LINNKPVEFE KLIPMEAPSL GVAIHS