ID   ASSY_YEAST              Reviewed;         420 AA.
AC   P22768; D6W209;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 3.
DT   24-JAN-2024, entry version 184.
DE   RecName: Full=Argininosuccinate synthase;
DE            EC=6.3.4.5 {ECO:0000269|PubMed:2897249, ECO:0000269|PubMed:35347};
DE   AltName: Full=Citrulline--aspartate ligase;
GN   Name=ARG1; OrderedLocusNames=YOL058W; ORFNames=O1228;
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=2123815; DOI=10.1016/0378-1119(90)90419-r;
RA   van Vliet F., Crabeel M., Boyen A., Tricot C., Stalon V., Falmagne P.,
RA   Nakamura Y., Baumberg S., Glansdorff N.;
RT   "Sequences of the genes encoding argininosuccinate synthetase in
RT   Escherichia coli and Saccharomyces cerevisiae: comparison with methanogenic
RT   archaebacteria and mammals.";
RL   Gene 95:99-104(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 90843 / S288c / FY73;
RX   PubMed=8789261;
RX   DOI=10.1002/(sici)1097-0061(199601)12:1<67::aid-yea884>3.0.co;2-f;
RA   Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.;
RT   "Analysis of a 26 kb region on the left arm of yeast chromosome XV.";
RL   Yeast 12:67-76(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [4]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 329-332.
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57, AND CATALYTIC ACTIVITY.
RX   PubMed=2897249; DOI=10.1007/bf00365645;
RA   Crabeel M., Seneca S., Devos K., Glansdorff N.;
RT   "Arginine repression of the Saccharomyces cerevisiae ARG1 gene. Comparison
RT   of the ARG1 and ARG3 control regions.";
RL   Curr. Genet. 13:113-124(1988).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=205532; DOI=10.1128/jb.133.3.1096-1107.1978;
RA   Jauniaux J.-C., Urrestarazu L.A., Wiame J.-M.;
RT   "Arginine metabolism in Saccharomyces cerevisiae: subcellular localization
RT   of the enzymes.";
RL   J. Bacteriol. 133:1096-1107(1978).
RN   [7]
RP   FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=35347; DOI=10.1111/j.1432-1033.1979.tb12882.x;
RA   Hilger F., Simon J.-P., Stalon V.;
RT   "Yeast argininosuccinate synthetase. Purification; structural and kinetic
RT   properties.";
RL   Eur. J. Biochem. 94:153-163(1979).
RN   [8]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [9]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Catalyzes the eighth step in arginine biosynthesis. Also has
CC       a catabolic function as the first enzyme of citrulline utilization as
CC       nitrogen source via arginine and the reactions involved in the arginase
CC       pathway. {ECO:0000269|PubMed:35347}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-
CC         arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743,
CC         ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000269|PubMed:2897249,
CC         ECO:0000269|PubMed:35347};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10933;
CC         Evidence={ECO:0000269|PubMed:2897249, ECO:0000269|PubMed:35347};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.1 mM for L-citrulline {ECO:0000269|PubMed:35347};
CC         KM=0.03 mM for L-aspartate {ECO:0000269|PubMed:35347};
CC         KM=0.3 mM for ATP {ECO:0000269|PubMed:35347};
CC       pH dependence:
CC         Optimum pH is 7.5-8.0 for the forward reaction and 6.0-6.5 for the
CC         reverse reaction. {ECO:0000269|PubMed:35347};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 2/3.
CC       {ECO:0000305|PubMed:2897249, ECO:0000305|PubMed:35347}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:35347}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:205532}.
CC   -!- MISCELLANEOUS: Present with 1870 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M35237; AAA34437.1; -; Genomic_DNA.
DR   EMBL; X91067; CAA62528.1; -; Genomic_DNA.
DR   EMBL; Z74800; CAA99067.1; -; Genomic_DNA.
DR   EMBL; X07070; CAA30106.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10725.2; -; Genomic_DNA.
DR   PIR; S59291; AJBYRS.
DR   RefSeq; NP_014583.2; NM_001183313.2.
DR   AlphaFoldDB; P22768; -.
DR   SMR; P22768; -.
DR   BioGRID; 34343; 28.
DR   DIP; DIP-1660N; -.
DR   IntAct; P22768; 5.
DR   MINT; P22768; -.
DR   STRING; 4932.YOL058W; -.
DR   iPTMnet; P22768; -.
DR   MaxQB; P22768; -.
DR   PaxDb; 4932-YOL058W; -.
DR   PeptideAtlas; P22768; -.
DR   EnsemblFungi; YOL058W_mRNA; YOL058W; YOL058W.
DR   GeneID; 854096; -.
DR   KEGG; sce:YOL058W; -.
DR   AGR; SGD:S000005419; -.
DR   SGD; S000005419; ARG1.
DR   VEuPathDB; FungiDB:YOL058W; -.
DR   eggNOG; KOG1706; Eukaryota.
DR   GeneTree; ENSGT00390000004524; -.
DR   HOGENOM; CLU_032784_4_2_1; -.
DR   InParanoid; P22768; -.
DR   OMA; QCEVVTF; -.
DR   OrthoDB; 350199at2759; -.
DR   BioCyc; YEAST:YOL058W-MONOMER; -.
DR   UniPathway; UPA00068; UER00113.
DR   BioGRID-ORCS; 854096; 8 hits in 10 CRISPR screens.
DR   PRO; PR:P22768; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P22768; Protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0004055; F:argininosuccinate synthase activity; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; IMP:SGD.
DR   GO; GO:0000053; P:argininosuccinate metabolic process; IBA:GO_Central.
DR   GO; GO:0000050; P:urea cycle; IBA:GO_Central.
DR   CDD; cd01999; Argininosuccinate_Synthase; 1.
DR   Gene3D; 3.90.1260.10; Argininosuccinate synthetase, chain A, domain 2; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00005; Arg_succ_synth_type1; 1.
DR   InterPro; IPR048268; Arginosuc_syn_C.
DR   InterPro; IPR048267; Arginosuc_syn_N.
DR   InterPro; IPR001518; Arginosuc_synth.
DR   InterPro; IPR018223; Arginosuc_synth_CS.
DR   InterPro; IPR023434; Arginosuc_synth_type_1_subfam.
DR   InterPro; IPR024074; AS_cat/multimer_dom_body.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00032; argG; 1.
DR   PANTHER; PTHR11587; ARGININOSUCCINATE SYNTHASE; 1.
DR   PANTHER; PTHR11587:SF2; ARGININOSUCCINATE SYNTHASE; 1.
DR   Pfam; PF20979; Arginosuc_syn_C; 1.
DR   Pfam; PF00764; Arginosuc_synth; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF69864; Argininosuccinate synthetase, C-terminal domain; 1.
DR   PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1.
DR   PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW   Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..420
FT                   /note="Argininosuccinate synthase"
FT                   /id="PRO_0000148559"
FT   BINDING         9..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000250"
FT   BINDING         114..122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        27..28
FT                   /note="GY -> AT (in Ref. 1; AAA34437 and 5; CAA30106)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        48..49
FT                   /note="EK -> VL (in Ref. 1; AAA34437 and 5; CAA30106)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61..64
FT                   /note="VDCR -> GGLS (in Ref. 1; AAA34437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169
FT                   /note="P -> F (in Ref. 1; AAA34437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        316
FT                   /note="F -> L (in Ref. 1; AAA34437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        329..332
FT                   /note="SYFT -> FLLH (in Ref. 1; AAA34437, 2; CAA62528 and
FT                   3; CAA99067)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   420 AA;  46928 MW;  155E1A4775B6FA9B CRC64;
     MSKGKVCLAY SGGLDTSVIL AWLLDQGYEV VAFMANVGQE EDFDAAKEKA LKIGACKFVC
     VDCREDFVKD ILFPAVQVNA VYEDVYLLGT SLARPVIAKA QIDVAKQEGC FAVSHGCTGK
     GNDQIRFELS FYALKPDVKC ITPWRMPEFF ERFAGRKDLL DYAAQKGIPV AQTKAKPWST
     DENQAHISYE AGILEDPDTT PPKDMWKLIV DPMDAPDQPQ DLTIDFERGL PVKLTYTDNK
     TSKEVSVTKP LDVFLAASNL ARANGVGRID IVEDRYINLK SRGCYEQAPL TVLRKAHVDL
     EGLTLDKEVR QLRDSFVTPN YSRLIYNGSY FTPECEYIRS MIQPSQNSVN GTVRVRLYKG
     NVIILGRSTK TEKLYDPTES SMDELTGFLP TDTTGFIAIQ AIRIKKYGES KKTKGEELTL
//