ID ASNS_CHICK Reviewed; 561 AA. AC Q5ZJU3; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 103. DE RecName: Full=Asparagine synthetase [glutamine-hydrolyzing]; DE EC=6.3.5.4; DE AltName: Full=Glutamine-dependent asparagine synthetase; GN Name=ASNS; ORFNames=RCJMB04_15l3; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=CB; TISSUE=Bursa of Fabricius; RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6; RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., RA Hayashizaki Y., Buerstedde J.-M.; RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene RT function analysis."; RL Genome Biol. 6:R6.1-R6.9(2005). 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; AJ720341; CAG32000.1; -; mRNA. DR RefSeq; NP_001026148.1; NM_001030977.1. DR RefSeq; XP_015136881.1; XM_015281395.1. DR RefSeq; XP_015136882.1; XM_015281396.1. DR RefSeq; XP_015136883.1; XM_015281397.1. DR AlphaFoldDB; Q5ZJU3; -. DR SMR; Q5ZJU3; -. DR BioGRID; 681517; 1. DR STRING; 9031.ENSGALP00000015846; -. DR MEROPS; C44.001; -. DR PaxDb; 9031-ENSGALP00000015846; -. DR Ensembl; ENSGALT00010007889.1; ENSGALP00010004735.1; ENSGALG00010003382.1. DR GeneID; 420574; -. DR KEGG; gga:420574; -. DR CTD; 440; -. DR VEuPathDB; HostDB:geneid_420574; -. DR eggNOG; KOG0571; Eukaryota. DR GeneTree; ENSGT00390000001994; -. DR InParanoid; Q5ZJU3; -. DR OMA; GIVCAFD; -. DR PhylomeDB; Q5ZJU3; -. DR UniPathway; UPA00134; UER00195. DR PRO; PR:Q5ZJU3; -. DR Proteomes; UP000000539; Chromosome 2. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006529; P:asparagine biosynthetic process; IBA:GO_Central. 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; 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; 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_0000056915" 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" SQ SEQUENCE 561 AA; 64097 MW; 94EFE934BED58FBF CRC64; MCGIWALFGS DECLSVQCLS AMKIAHRGPD AFRFENVNGF TNCCFGFHRL AVVDQLYGMQ PIRVKKFPYL WLCYNGEIYN FKQLQEQFGF EYQTLVDGEV ILHLYNRGGI EQTASMLDGV FAFILLDTAN RKVFLARDTY GVRPLFKVLT DDGFLGVCSE AKGLINLKHS TSLFPKVEPF LPGHYEVLDL KPSGKVVSVE VVKFHSYKDE PLHAACDTVG NLPSGFDLET VKSNIRVLFE NAVRKRLMAH RRIGCLLSGG LDSSLVAAVL LKLMKEMNIK YPLQTFAIGM ENSPDLLAAR KVAAHIGSEH HEVIFNSEEG IQAVEEVIFS LETYDITTVR ASIGMYLVSK YIRKKTDSVV IFSGEGSDEL TQGYIYFHKA PSPEEAAEES ERLLKELYLF DVLRADRTTA AHGLELRVPF LDHRFTSYYL SLPAELRIPK NGIEKYLLRQ SFEDSNLLPK EILWRPKEAF SDGIASVKKS WFSILQDYID QQVDDLLLEK AAEKYPFNPP RTKESYYYRQ IFEKHYPGRS SWLPHYWMPR WVEATDPSAR TLKHYKSAIQ E //