ID ASNS_MESAU Reviewed; 561 AA. AC P17714; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 114. DE RecName: Full=Asparagine synthetase [glutamine-hydrolyzing]; DE EC=6.3.5.4; DE AltName: Full=Glutamine-dependent asparagine synthetase; GN Name=ASNS; OS Mesocricetus auratus (Golden hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; OC Cricetidae; Cricetinae; Mesocricetus. OX NCBI_TaxID=10036; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTANTS TS11. RC STRAIN=Syrian; RX PubMed=1972978; DOI=10.1093/nar/18.12.3509; RA Gong S.S., Basilico C.; RT "A mammalian temperature-sensitive mutation affecting G1 progression RT results from a single amino acid substitution in asparagine synthetase."; RL Nucleic Acids Res. 18:3509-3513(1990). 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 -!- MISCELLANEOUS: The temperature-sensitive mutation affecting G1 CC progression results from a single amino acid substitution. 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; X52130; CAA36375.1; -; mRNA. DR PIR; S12740; AJHYNG. DR RefSeq; NP_001268543.1; NM_001281614.1. DR AlphaFoldDB; P17714; -. DR SMR; P17714; -. DR STRING; 10036.ENSMAUP00000003671; -. DR MEROPS; C44.974; -. DR GeneID; 101836926; -. DR KEGG; maua:101836926; -. DR CTD; 440; -. DR OrthoDB; 684401at2759; -. DR UniPathway; UPA00134; UER00195. DR Proteomes; UP000189706; Unplaced. 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:SF23; ASPARAGINE SYNTHETASE [GLUTAMINE-HYDROLYZING]; 1. DR Pfam; PF00733; Asn_synthase; 2. 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 1: Evidence at protein level; KW Acetylation; Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding; KW Glutamine amidotransferase; Ligase; Nucleotide-binding; Phosphoprotein; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..561 FT /note="Asparagine synthetase [glutamine-hydrolyzing]" FT /id="PRO_0000056911" FT DOMAIN 2..191 FT /note="Glutamine amidotransferase type-2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609" FT DOMAIN 213..536 FT /note="Asparagine synthetase" FT ACT_SITE 2 FT /note="For GATase activity" FT /evidence="ECO:0000250" FT BINDING 49..53 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 97 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250" FT BINDING 256 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 288 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 363..364 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT SITE 365 FT /note="Important for beta-aspartyl-AMP intermediate FT formation" FT /evidence="ECO:0000250" FT MOD_RES 385 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P08243" FT MOD_RES 545 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P08243" FT MOD_RES 557 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08243" FT MUTAGEN 414 FT /note="L->F: In ts11; temperature-sensitive. Blocked in the FT G1 phase of the cell cycle at the non-permissive FT temperature (39.5 degrees Celsius). Heat labile." SQ SEQUENCE 561 AA; 64274 MW; 69DF791ED0FA0EF0 CRC64; MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDPLFGMQ PIRVKKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI ILHLYDKGGI EQTICMLDGV FAFILLDTAN KKVFLGRDTY GVRPLFKAMT EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF LPGHYEVLDL KPNGKVASVE MVKYHHCRDE PLHALYDSVE KLFPGFELET VKSNLRILFD NAVRKRLMTD RRIVCLLSGG LDSSLVASSL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR KVANYIGSEH HEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPEMRVPK NGIEKHLLRE TFEDSNLLPK EILWRPKEAF SDGITSVKNS WFKILQDYVE HQVDDAMMAT AAQKFPFNTP KTKEGYFYRQ IFEHHYPGRA DWLTHYWMPK WINATDPSAR TLTHYKSAAK A //