ID ASNS_CRIGR Reviewed; 561 AA. AC P19891; Q6LBT9; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 129. DE RecName: Full=Asparagine synthetase [glutamine-hydrolyzing]; DE EC=6.3.5.4; DE AltName: Full=Glutamine-dependent asparagine synthetase; GN Name=ASNS; Synonyms=AS; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; OC Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Ovary; RX PubMed=2477309; DOI=10.1016/0378-1119(89)90252-7; RA Andrulis I.L., Shotwell M., Evans-Blackler S., Zalkin H., Siminovitch L., RA Ray P.N.; RT "Fine structure analysis of the Chinese hamster AS gene encoding asparagine RT synthetase."; RL Gene 80:75-85(1989). 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 --------------------------------------------------------------------------- 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; M27838; AAA36977.1; -; mRNA. DR EMBL; X12950; CAA31409.1; -; mRNA. DR PIR; JS0273; AJHYNC. DR RefSeq; XP_003509834.1; XM_003509786.3. DR RefSeq; XP_003509835.1; XM_003509787.3. DR RefSeq; XP_007630216.1; XM_007632026.2. DR RefSeq; XP_007630217.1; XM_007632027.2. DR AlphaFoldDB; P19891; -. DR SMR; P19891; -. DR MEROPS; C44.974; -. DR PaxDb; 10029-XP_007630216-1; -. DR Ensembl; ENSCGRT00000015762; ENSCGRP00000015531; ENSCGRG00000011278. DR Ensembl; ENSCGRT00001018823.1; ENSCGRP00001014586.1; ENSCGRG00001015428.1. DR Ensembl; ENSCGRT00015041707; ENSCGRP00015034196; ENSCGRG00015025770. DR GeneID; 100760225; -. DR CTD; 440; -. DR eggNOG; KOG0571; Eukaryota. DR GeneTree; ENSGT00390000001994; -. DR OMA; HYLNFHA; -. DR OrthoDB; 684401at2759; -. DR UniPathway; UPA00134; UER00195. DR Proteomes; UP000694386; Unplaced. DR Proteomes; UP001108280; Genome assembly. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. 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:0042149; P:cellular response to glucose starvation; IEA:Ensembl. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl. 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 2: Evidence at transcript level; KW Acetylation; Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding; KW Glutamine amidotransferase; Ligase; Nucleotide-binding; Phosphoprotein. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..561 FT /note="Asparagine synthetase [glutamine-hydrolyzing]" FT /id="PRO_0000056909" 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" SQ SEQUENCE 561 AA; 64327 MW; AB879821C42C5D1B CRC64; MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDPLFGMQ PIRVKKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI ILHLYDKGGI EQTICMLDGV FAFILLDTAN KKVFLGRDTY GVRPLFKAMT EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF LPGHYEVLDL KPNGKVASVE MVKYHHCRDE PLHALYDSVE KLFQGFELET VKSNLRILFD SAVRKRLMTD RRIGCLLSGG LDSSLVAASL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR KVANYIGSEH HEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPEMRIPK NGIEKHLLRE TFEDSNLLPK EILWRPKEAF SDGITSVKNS WFKILQDYVE HQVDDEMMAT AAQKFPFNTP KTKEGYYYRQ IFERHYPGRA DWLTHYWMPK WINATDPSAR TLTHYKSAAK A //