ID A0A446U4J3_TRITD Unreviewed; 511 AA. AC A0A446U4J3; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 19-JAN-2022, entry version 14. DE RecName: Full=Asparagine synthetase [glutamine-hydrolyzing] {ECO:0000256|PIRNR:PIRNR001589}; DE EC=6.3.5.4 {ECO:0000256|PIRNR:PIRNR001589}; GN ORFNames=TRITD_5Bv1G097460 {ECO:0000313|EMBL:VAI30543.1}; OS Triticum turgidum subsp. durum (Durum wheat) (Triticum durum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum. OX NCBI_TaxID=4567 {ECO:0000313|EMBL:VAI30543.1, ECO:0000313|Proteomes:UP000324705}; RN [1] {ECO:0000313|EMBL:VAI30543.1, ECO:0000313|Proteomes:UP000324705} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG International Durum Wheat Genome Sequencing Consortium (IDWGSC); RA Milanesi L.; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. 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 Evidence={ECO:0000256|ARBA:ARBA00001778, CC ECO:0000256|PIRNR:PIRNR001589}; 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; LT934120; VAI30543.1; -; Genomic_DNA. DR Proteomes; UP000324705; Chromosome 5b. 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:0006529; P:asparagine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. 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; 2. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR01536; asn_synth_AEB; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. PE 4: Predicted; KW Amino-acid biosynthesis {ECO:0000256|PIRSR:PIRSR001589-1}; KW Asparagine biosynthesis {ECO:0000256|PIRSR:PIRSR001589-1}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001589}; KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962, KW ECO:0000256|PIRSR:PIRSR001589-1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRNR:PIRNR001589}; KW Reference proteome {ECO:0000313|Proteomes:UP000324705}. FT DOMAIN 2..185 FT /note="Glutamine amidotransferase type-2" FT /evidence="ECO:0000259|PROSITE:PS51278" FT NP_BIND 341..342 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2" FT ACT_SITE 2 FT /note="For GATase activity" FT /evidence="ECO:0000256|PIRSR:PIRSR001589-1" FT BINDING 98 FT /note="Glutamine" FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2" FT BINDING 231 FT /note="ATP; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2" FT BINDING 267 FT /note="ATP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2" FT SITE 343 FT /note="Important for beta-aspartyl-AMP intermediate FT formation" FT /evidence="ECO:0000256|PIRSR:PIRSR001589-3" SQ SEQUENCE 511 AA; 57924 MW; CDB93B7BAA856647 CRC64; MCGILAVLGC ADDTQGKRVR VLELSRRLKH RGPDWSGMHQ VGDCYLSHQR LAIIDPASGD QPLYNEDKSI VVTVNGEIYN HEQLRAQLSS HTFRTGSDCE VIAHLYEEHG ENFIDMLDGV FSFVLLDTRD NSFIAARDAI GVTPLYIGWG IDGSVWISSE MKGLNDDCEH FEIFPPGHLY SSKQGGFKRW YNPPWFSEVI PSVPYDPLAL RKAFEKAVVK RLMTDVPFGV LLSGGLDSSL VAAVTVRHLA GTKAAKRWGT KLHSFCVGLE GSPDLKAAKE VANYLGTMHH EFTFTVQDGI DAIEDVIYHT ETYDVTTIRA STPMFLMSRK IKSLGVKMVI SGEGSDEIFG GYLYFHKAPN KEELHRETCQ KIKALHQYDC LRANKATSAW GLEARVPFLD KEFINEAMSI DPEWKMIRPD LGRIEKWVLR KAFDDEEQPF LPKHILYRQK EQFSDGVGYS WIDGLKAHAE SNVTDKMMSN AKFIYPHNTP TTKEAYCYRM IFERFFPQVS K //