ID   ASNS_MAIZE              Reviewed;         586 AA.
AC   P49094;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Asparagine synthetase [glutamine-hydrolyzing];
DE            EC=6.3.5.4;
DE   AltName: Full=Glutamine-dependent asparagine synthetase;
GN   Name=ASN1; Synonyms=AS;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. DEA; TISSUE=Root meristem;
RX   PubMed=8580967; DOI=10.1046/j.1365-313x.1996.09010001.x;
RA   Chevalier C., Bourgeois E., Just D., Raymond P.;
RT   "Metabolic regulation of asparagine synthetase gene expression in maize
RT   (Zea mays L.) root tips.";
RL   Plant J. 9:1-11(1996).
CC   -!- FUNCTION: Essential for nitrogen assimilation, distribution and
CC       remobilization within the plant via the phloem. {ECO:0000250}.
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; X82849; CAA58052.1; -; mRNA.
DR   PIR; T02978; T02978.
DR   AlphaFoldDB; P49094; -.
DR   SMR; P49094; -.
DR   STRING; 4577.GRMZM2G074589_P01; -.
DR   PRIDE; P49094; -.
DR   MaizeGDB; 79071; -.
DR   UniPathway; UPA00134; UER00195.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P49094; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006529; P:asparagine biosynthetic process; IBA:GO_Central.
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; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..586
FT                   /note="Asparagine synthetase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000056924"
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;  66578 MW;  72772722DEEFA222 CRC64;
     MCGILAVLGV VEVSLAKRSR IIELSRRLRH RGPDWSGLHC HEDCYLAHQR LAIIDPTSGD
     QPLYNEDKTV VVTVNGEIYN HEELKAKLKT HEFQTGSDCE VIAHLYEEYG EEFVDMLDGM
     FSFVLLDTRD KSFIAARDAI GICPLYMGWG LDGSVWFSSE MKALSDDCER FITFPPGHLY
     SSKTGGLRRW YNPPWFSETV PSTPYNALFL REMFEKAVIK RLMTDVPFGV LLSGGLDSSL
     VASVASRHLN ETKVDRQWGN KLHTFCIGLK GSPDLKAARE VADYLSTVHH EFHFTVQEGI
     DALEEVIYHI ETYDVTTIRA STPMFLMSRK IKSLGVKMVI SGEGSDEIFG GYLYFHKAPN
     KKEFLEETCR KIKALHLYDC LRANKATSAW GVEARVPFLD KSFISVAMDI DPEWNMIKRD
     LGRIEKWVMR KAFDDDEHPY LPKHILYRQK EQFSDGVGYN WIDGLKSFTE QQVTDEMMNN
     AAQMFPYNTP VNKEAYYYRM IFERLFPQDS ARETVPWGPS IACSTPAAIE WVEQWKASND
     PSGRFISSHD SAATDHTAVS RRWPTAAARP ANGTVNGKDV PVPIAV