ASNS2_PEA
ID ASNS2_PEA Reviewed; 583 AA.
AC P19252; O49926;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Asparagine synthetase, root [glutamine-hydrolyzing];
DE EC=6.3.5.4;
DE AltName: Full=Glutamine-dependent asparagine synthetase;
GN Name=AS2;
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;
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 [GENOMIC DNA] 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: Roots.
CC -!- INDUCTION: By darkness.
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; X52180; CAA36430.1; -; mRNA.
DR EMBL; Y13322; CAA73763.1; -; Genomic_DNA.
DR PIR; S11443; AJPMN2.
DR AlphaFoldDB; P19252; -.
DR SMR; P19252; -.
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..583
FT /note="Asparagine synthetase, root [glutamine-hydrolyzing]"
FT /id="PRO_0000056927"
FT DOMAIN 2..185
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 237..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"
FT CONFLICT 34
FT /note="E -> D (in Ref. 2; CAA73763)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="Y -> F (in Ref. 2; CAA73763)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="Q -> H (in Ref. 2; CAA73763)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="I -> L (in Ref. 2; CAA73763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 65650 MW; E2C2DA6FEF1C72F1 CRC64;
MCGILAVLGC SDPSRAKRVR VLELSRRLKH RGPEWSGLHQ HGDCYLAQQR LAIVDPASGD
QPLFNEDNPS IVTVNGEIYN HEDLRKQLSN HTFRTGSDCD VIAHLYEEYG EDFVDMLDGI
FSFVPLDTRD NSYIVARDAI GVTSLYIGWG LDGSVWISSE MKGLNDDCEH FECFPPGHLY
SSKDSGFRRW YNPSWYSEAI PSAPYDPLAL RHAFEKAVVK RLMTDVPFGV LLSGGLDSSL
VASITSRYLA TTKAAEQWGS KLHSFCVGLE GSPDLKAGKE VADYLGTVHH EFTFTVQDGI
DAIEDVIYHV ETYDVTSIRA STPMFLMSRK IKSLGVKWVI SGEGSDEIFG GYLYFHKAPN
KEEFHEETCR KIKALHQYDC QRANKSTYAW GLEARVPFLD KAFINVAMNI DPENKMIKRD
EGRIEKYILR KAFDDEENPY LPKHILYRQK EQFSDGVGYS WIDGLKAHAA KHVTDKMMLN
AGNIFPHNTP NTKEAYYYRM IFERFFPQNS ARLTVPGGPT VACSTAKAVE WDAAWSNNLD
PSGRAALGVH DSAYENHNKV NKTVEFEKII PLEAAPVELA IQG
