ID A0A446U4J3_TRITD Unreviewed; 511 AA. AC A0A446U4J3; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 31-JUL-2019, entry version 4. 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}; RN [1] {ECO:0000313|EMBL:VAI30543.1} RP NUCLEOTIDE SEQUENCE. RG International Durum Wheat Genome Sequencing Consortium (IDWGSC); RA Milanesi L.; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:VAI30543.1} RP NUCLEOTIDE SEQUENCE. RG XXX; RL Submitted (JUL-2018) 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; CC EC=6.3.5.4; Evidence={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 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|PIRNR:PIRNR001589, KW ECO:0000256|PIRSR:PIRSR001589-2}; KW Glutamine amidotransferase {ECO:0000256|PIRSR:PIRSR001589-1}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001589, KW ECO:0000256|PIRSR:PIRSR001589-2}. FT DOMAIN 2 185 Glutamine amidotransferase type-2. FT {ECO:0000259|PROSITE:PS51278}. FT NP_BIND 341 342 ATP. {ECO:0000256|PIRSR:PIRSR001589-2}. FT ACT_SITE 2 2 For GATase activity. {ECO:0000256|PIRSR: FT PIRSR001589-1}. FT BINDING 98 98 Glutamine. {ECO:0000256|PIRSR: FT PIRSR001589-2}. FT BINDING 231 231 ATP; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR001589-2}. FT BINDING 267 267 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR001589- FT 2}. FT SITE 343 343 Important for beta-aspartyl-AMP FT intermediate formation. FT {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 //