ASNS1_YEAST
ID ASNS1_YEAST Reviewed; 572 AA.
AC P49089; D6W4E2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Asparagine synthetase [glutamine-hydrolyzing] 1;
DE EC=6.3.5.4;
DE AltName: Full=Glutamine-dependent asparagine synthetase 1;
GN Name=ASN1; OrderedLocusNames=YPR145W; ORFNames=P9659.3;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8951815; DOI=10.1046/j.1365-2958.1996.d01-1715.x;
RA Dang V.D., Valens M., Bolotin-Fukuhara M., Daignan-Fornier B.;
RT "Cloning of the ASN1 and ASN2 genes encoding asparagine synthetases in
RT Saccharomyces cerevisiae: differential regulation by the CCAAT-box-binding
RT factor.";
RL Mol. Microbiol. 22:681-692(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265 AND SER-509, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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; Z48675; CAA88594.1; -; Genomic_DNA.
DR EMBL; U40829; AAB68284.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11558.1; -; Genomic_DNA.
DR PIR; S52694; S52694.
DR RefSeq; NP_015471.1; NM_001184242.1.
DR AlphaFoldDB; P49089; -.
DR SMR; P49089; -.
DR BioGRID; 36314; 77.
DR DIP; DIP-3810N; -.
DR IntAct; P49089; 3.
DR STRING; 4932.YPR145W; -.
DR iPTMnet; P49089; -.
DR MaxQB; P49089; -.
DR PaxDb; P49089; -.
DR PRIDE; P49089; -.
DR EnsemblFungi; YPR145W_mRNA; YPR145W; YPR145W.
DR GeneID; 856268; -.
DR KEGG; sce:YPR145W; -.
DR SGD; S000006349; ASN1.
DR VEuPathDB; FungiDB:YPR145W; -.
DR eggNOG; KOG0571; Eukaryota.
DR GeneTree; ENSGT00940000171863; -.
DR HOGENOM; CLU_014658_2_2_1; -.
DR InParanoid; P49089; -.
DR OMA; DWSGIYS; -.
DR BioCyc; YEAST:YPR145W-MON; -.
DR Reactome; R-SCE-8963693; Aspartate and asparagine metabolism.
DR UniPathway; UPA00134; UER00195.
DR PRO; PR:P49089; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P49089; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006529; P:asparagine biosynthetic process; IGI:SGD.
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; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..572
FT /note="Asparagine synthetase [glutamine-hydrolyzing] 1"
FT /id="PRO_0000056917"
FT DOMAIN 2..186
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 194..546
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 74..76
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 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 366..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 368
FT /note="Important for beta-aspartyl-AMP intermediate
FT formation"
FT /evidence="ECO:0000250"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 572 AA; 64470 MW; 39F2873F0E689FC9 CRC64;
MCGIFAAFRH EDVHRYKPKA LQLSKRIRHR GPDWSGNAIK NSTIFVHERL AIVGVESGAQ
PITSSDGEYM LCVNGEIYNH IQLREECADY EFGTLSDCEP IIPMYLKHDI DAPKYLDGMF
AWTLYDAKQD RIVAARDPIG ITTLYMGRSS ASPKTVYFAS ELKCLTDDCD TITAFPPGHV
YDSKTDKITR YFTPDWLDEK RIPSTPIDYM AIRHSLEKAV RKRLMAEVPY GVLLSGGLDS
SLIASIAARE TAKATNDVEP STYDSKARHL AGIDDDGKLH TAGWTSLHSF AIGLPNAPDL
QAARKVAKFI GSIHHEHTFT LQEGLDALDD VIYHLETYDV TTIRASTPMF LLSRKIKAQG
VKMVLSGEGS DEIFGGYLYF AQAPSAAEFH TESVQRVKNL HLADCLRANK STMAWGLEAR
VPFLDREFLQ LCMNIDPNEK MIKPKEGRIE KYILRKAFDT TGEPDAKPYL PEEILWRQKE
QFSDGVGYSW IDGLKDTAEA VISDEMFASP KAEWGSDIPT TKEAFWYRLK FDALFPQKTV
ADTVMRWIPK ADWGCAEDPS GRYAQIHEKH IE
