ASSY_YEAST
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 03-AUG-2022, entry version 178.
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}.
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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; 23.
DR DIP; DIP-1660N; -.
DR IntAct; P22768; 5.
DR MINT; P22768; -.
DR STRING; 4932.YOL058W; -.
DR iPTMnet; P22768; -.
DR MaxQB; P22768; -.
DR PaxDb; P22768; -.
DR PRIDE; P22768; -.
DR EnsemblFungi; YOL058W_mRNA; YOL058W; YOL058W.
DR GeneID; 854096; -.
DR KEGG; sce:YOL058W; -.
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 BioCyc; YEAST:YOL058W-MON; -.
DR UniPathway; UPA00068; UER00113.
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; 3.40.50.620; -; 1.
DR Gene3D; 3.90.1260.10; -; 1.
DR HAMAP; MF_00005; Arg_succ_synth_type1; 1.
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 PANTHER; PTHR11587; PTHR11587; 1.
DR Pfam; PF00764; Arginosuc_synth; 1.
DR SUPFAM; SSF69864; SSF69864; 1.
DR TIGRFAMs; TIGR00032; argG; 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
