ASNS_DICDI
ID ASNS_DICDI Reviewed; 557 AA.
AC Q54MB4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable asparagine synthetase [glutamine-hydrolyzing];
DE EC=6.3.5.4;
DE AltName: Full=Glutamine-dependent asparagine synthetase;
GN Name=asns; Synonyms=asnA; ORFNames=DDB_G0286059;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
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; AAFI02000085; EAL64408.1; -; Genomic_DNA.
DR RefSeq; XP_637920.1; XM_632828.1.
DR AlphaFoldDB; Q54MB4; -.
DR SMR; Q54MB4; -.
DR STRING; 44689.DDB0230140; -.
DR MEROPS; C44.001; -.
DR PaxDb; Q54MB4; -.
DR PRIDE; Q54MB4; -.
DR EnsemblProtists; EAL64408; EAL64408; DDB_G0286059.
DR GeneID; 8625431; -.
DR KEGG; ddi:DDB_G0286059; -.
DR dictyBase; DDB_G0286059; asns.
DR eggNOG; KOG0571; Eukaryota.
DR HOGENOM; CLU_014658_2_2_1; -.
DR InParanoid; Q54MB4; -.
DR OMA; DWSGIYS; -.
DR PhylomeDB; Q54MB4; -.
DR Reactome; R-DDI-8963693; Aspartate and asparagine metabolism.
DR UniPathway; UPA00134; UER00195.
DR PRO; PR:Q54MB4; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; ISS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006529; P:asparagine biosynthetic process; ISS:dictyBase.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein 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..557
FT /note="Probable asparagine synthetase [glutamine-
FT hydrolyzing]"
FT /id="PRO_0000329451"
FT DOMAIN 2..188
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 217..466
FT /note="Asparagine synthetase"
FT REGION 538..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 50..54
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 101
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 353..354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 355
FT /note="Important for beta-aspartyl-AMP intermediate
FT formation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 557 AA; 63487 MW; 02E7F990A55CA254 CRC64;
MCGILAILNS LEEASKLRKK ALSLSSRLRH RGPDWNGIYQ SSDSILTHER LAIVGLENGA
QPLLNEDETI ALTVNGEIYN HEKLREDLVA TGKHTFKTHS DCEPILHLYE DKGDDFVHML
DGDFAFVVYN KKANSFLAAR DPIGVVPLYI GWHKDGSIWF SSEMKAIKDD CYKFQPFPPG
HYFSSKTKEF VRYYKPNWIM GDSPSGVLKS EEQVLPAIKE AFEQAVVSRM MSDVPYGVLL
SGGLDSSLVA SIVSRHAEQR VEDHEKSRAW WPRIHSFCIG LKDAPDLKAA RDVADYLQTV
HHEYHFTVQE GIDALPDVIK HLETYDVTTI RASTPMYFLS RKIKAMGVKM VLSGEGSDEI
FGGYLYFHNA PDANEFHVEC CRRIKALHSF DCLRANKSTA AWGVEVRVPF LDQRFLDVAM
NIDPSHKVCH DDQGKKRMEK YILRKAFETK EGEKPYLPSS VLWRQKEQFS DGVGYSWIDG
LKENAENEVS DEEFAKRESY FPDDTPTTKE AFLYRKMFEA IYPGKECMET VQRWIPTWGA
SQDPSGRAQK VHLSTTE
