ASNS_BOVIN
ID ASNS_BOVIN Reviewed; 561 AA.
AC Q1LZA3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Asparagine synthetase [glutamine-hydrolyzing];
DE EC=6.3.5.4;
DE AltName: Full=Glutamine-dependent asparagine synthetase;
GN Name=ASNS;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) 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; 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; BC116123; AAI16124.1; -; mRNA.
DR RefSeq; NP_001069121.1; NM_001075653.1.
DR RefSeq; XP_015323612.1; XM_015468126.1.
DR AlphaFoldDB; Q1LZA3; -.
DR SMR; Q1LZA3; -.
DR STRING; 9913.ENSBTAP00000004181; -.
DR PaxDb; Q1LZA3; -.
DR PeptideAtlas; Q1LZA3; -.
DR PRIDE; Q1LZA3; -.
DR Ensembl; ENSBTAT00000004181; ENSBTAP00000004181; ENSBTAG00000003222.
DR Ensembl; ENSBTAT00000069847; ENSBTAP00000069683; ENSBTAG00000003222.
DR Ensembl; ENSBTAT00000079655; ENSBTAP00000068704; ENSBTAG00000003222.
DR GeneID; 514209; -.
DR KEGG; bta:514209; -.
DR CTD; 440; -.
DR VEuPathDB; HostDB:ENSBTAG00000003222; -.
DR eggNOG; KOG0571; Eukaryota.
DR GeneTree; ENSGT00390000001994; -.
DR HOGENOM; CLU_014658_2_1_1; -.
DR InParanoid; Q1LZA3; -.
DR OMA; DWSGIYS; -.
DR OrthoDB; 782607at2759; -.
DR TreeFam; TF300603; -.
DR Reactome; R-BTA-8963693; Aspartate and asparagine metabolism.
DR UniPathway; UPA00134; UER00195.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000003222; Expressed in oocyte and 108 other tissues.
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; 1.
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 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_0000269563"
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"
SQ SEQUENCE 561 AA; 64220 MW; 71379296556DB3D1 CRC64;
MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDQLFGMQ
PIRVKKYPYL WLCYNGEIYN HKKLQHHFEF EYQTKVDGEI ILHLYDKGGI EQTVCMLDGV
FAFILLDTAN KKVFLGRDTY GVRPLFKAMT EDGFLAVCSE AKGLVNLKHS MTPFLKVEPF
LPGHYEVLDL KPNGKVASVE MVKHHHCRDE PLHALYDGVE KLFPGFEIET VKSNLRILFD
NAVKKRLMTD RRIGCLLSGG LDSSLVAATL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR
KVANHIGSEH HEVLFNSEEG IQVLDEVIFS LETYDITTVR ASVGMYLISK YIRKNTDSVV
IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLRELYLF DVLRADRTTA AHGLELRVPF
LDHRFSSYYL SLPPDMRVPK NGIEKHLLRE TFEDSNLIPK EILWRPKEAF SDGITSVKNS
WFRILQDYIE HQVDDAAMAS AAQKFPINTP KTKEGYYYRQ IFENHYPGRA DWLPHYWMPR
WTNATDPSAR TLTHYKAAAK A
