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   27-MAR-2024, entry version 112.
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.ENSBTAP00000068704; -.
DR   PaxDb; 9913-ENSBTAP00000004181; -.
DR   PeptideAtlas; Q1LZA3; -.
DR   Ensembl; ENSBTAT00000004181.5; ENSBTAP00000004181.4; ENSBTAG00000003222.5.
DR   Ensembl; ENSBTAT00000069847.1; ENSBTAP00000069683.1; ENSBTAG00000003222.5.
DR   Ensembl; ENSBTAT00000079655.1; ENSBTAP00000068704.1; ENSBTAG00000003222.5.
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; GIVCAFD; -.
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 cell types or 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; 3.60.20.10; 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;
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
//