ID   ASNS1_PEA               Reviewed;         586 AA.
AC   P19251; O49925;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Asparagine synthetase, nodule [glutamine-hydrolyzing];
DE            EC=6.3.5.4;
DE   AltName: Full=Glutamine-dependent asparagine synthetase;
GN   Name=AS1;
OS   Pisum sativum (Garden pea).
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; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Sparkle; TISSUE=Root nodule;
RX   PubMed=1968003; DOI=10.1002/j.1460-2075.1990.tb08114.x;
RA   Tsai F.Y., Coruzzi G.M.;
RT   "Dark-induced and organ-specific expression of two asparagine synthetase
RT   genes in Pisum sativum.";
RL   EMBO J. 9:323-332(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 1-84.
RC   STRAIN=cv. Feltham First;
RX   PubMed=9418044; DOI=10.1046/j.1365-313x.1997.12051021.x;
RA   Ngai N., Tsai F.Y., Coruzzi G.M.;
RT   "Light-induced transcriptional repression of the pea AS1 gene:
RT   identification of cis-elements and transfactors.";
RL   Plant J. 12:1021-1034(1997).
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   -!- TISSUE SPECIFICITY: Root nodules.
CC   -!- INDUCTION: By darkness.
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DR   EMBL; X52179; CAA36429.1; -; mRNA.
DR   EMBL; Y13321; CAA73762.1; -; Genomic_DNA.
DR   PIR; S11444; AJPMN1.
DR   AlphaFoldDB; P19251; -.
DR   SMR; P19251; -.
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..586
FT                   /note="Asparagine synthetase, nodule [glutamine-
FT                   hydrolyzing]"
FT                   /id="PRO_0000056926"
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         232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         342..343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            344
FT                   /note="Important for beta-aspartyl-AMP intermediate
FT                   formation"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   586 AA;  66353 MW;  17C5019A3C8ED491 CRC64;
     MCGILAVLGC SDDSQAKRVR ILELSRRLKH RGPDWSGLHQ HGDNYLAHQR LAIVDPASGD
     QPLFNEDKSI IVTVNGEIYN HEELRKQLPN HKFFTQCDCD VIAHLYEEHG ENFVDMLDGI
     FSFVLLDTRD NSFIVARDAI GVTSLYIGWG LDGSVWIASE LKGLNDECEH FEVFPPGHLY
     SSKEREFRRW YNPPWFNEAI IPSTPYDPLV LRNAFEKAVI KRLMTDVPFG VLLSGGLDSS
     LVASVTARYL AGTKAAKQWG AKLPSFCVGL KGAPDLKAGK EVADFLGTVH HEFEFTIQDG
     IDAIEDVIYH TETYDVTTIR AATPMFLMSR KIKSSGVKWV ISGEGSDEIF GGYLYFHKAP
     NREEFHQETC RKIKALHRYD CLRANKSTYA WGLEARVPFL DKDFIKVAMD IDPEFKMIKH
     DEGRIEKWIL RKAFDDEENP YLPKHILYRQ KEQFSDGVGY GWIDGIKDHA AKHVTDRMMF
     NASHIFPFNT PNTKEAYYYR MIFERFFPQN SARLTVPGGP SVACSTEKAI EWDASWSNNL
     DPSGRAALGV HVSAYEHQIN PVTKGVEPEK IIPKIGVSPL GVAIQT