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 24-JAN-2024, entry version 112. 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) (Lathyrus oleraceus). 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; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1. DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR01536; asn_synth_AEB; 1. DR PANTHER; PTHR11772; ASPARAGINE SYNTHETASE; 1. DR PANTHER; PTHR11772:SF45; ASPARAGINE SYNTHETASE [GLUTAMINE-HYDROLYZING]; 1. DR Pfam; PF00733; Asn_synthase; 1. DR Pfam; PF13537; GATase_7; 1. DR PIRSF; PIRSF001589; Asn_synthetase_glu-h; 1. DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 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 //