ASNS_CRIGR
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 03-AUG-2022, entry version 121.
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.
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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 STRING; 10029.XP_007630216.1; -.
DR MEROPS; C44.974; -.
DR Ensembl; ENSCGRT00001018823; ENSCGRP00001014586; ENSCGRG00001015428.
DR GeneID; 100760225; -.
DR KEGG; cge:100760225; -.
DR CTD; 440; -.
DR eggNOG; KOG0571; Eukaryota.
DR GeneTree; ENSGT00390000001994; -.
DR OMA; DIHTWMR; -.
DR OrthoDB; 782607at2759; -.
DR UniPathway; UPA00134; UER00195.
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; 3.40.50.620; -; 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.
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
