ASNS_CHICK
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 03-AUG-2022, entry version 96.
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.
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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; Q5ZJU3; -.
DR PRIDE; Q5ZJU3; -.
DR GeneID; 420574; -.
DR KEGG; gga:420574; -.
DR CTD; 440; -.
DR VEuPathDB; HostDB:geneid_420574; -.
DR eggNOG; KOG0571; Eukaryota.
DR InParanoid; Q5ZJU3; -.
DR OrthoDB; 782607at2759; -.
DR PhylomeDB; Q5ZJU3; -.
DR UniPathway; UPA00134; UER00195.
DR PRO; PR:Q5ZJU3; -.
DR Proteomes; UP000000539; Unplaced.
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; 3.40.50.620; -; 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; 2.
DR Pfam; PF13537; GATase_7; 1.
DR PIRSF; PIRSF001589; Asn_synthetase_glu-h; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01536; asn_synth_AEB; 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
