ID   ARLY_YEAST              Reviewed;         463 AA.
AC   P04076; D3DKW3;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   04-NOV-2026, entry version 213.
DE   RecName: Full=Argininosuccinate lyase;
DE            Short=ASAL;
DE            EC=4.3.2.1;
DE   AltName: Full=Arginosuccinase;
GN   Name=ARG4; OrderedLocusNames=YHR018C;
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=6386606; DOI=10.1016/0378-1119(84)90056-8;
RA   Beacham I.R., Schweitzer B.W., Warrick H.M., Carbon J.;
RT   "The nucleotide sequence of the yeast ARG4 gene.";
RL   Gene 29:271-279(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176.
RX   PubMed=3889658; DOI=10.1038/315350a0;
RA   White J.H., Lusnak K., Fogel S.;
RT   "Mismatch-specific post-meiotic segregation frequency in yeast suggests a
RT   heteroduplex recombination intermediate.";
RL   Nature 315:350-352(1985).
RN   [6]
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).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP   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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine;
CC         Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:57472; EC=4.3.2.1;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 3/3.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- MISCELLANEOUS: Present with 10200 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M36586; AAA34435.1; -; Genomic_DNA.
DR   EMBL; K01813; AAA34434.1; -; Genomic_DNA.
DR   EMBL; AY693155; AAT93174.1; -; Genomic_DNA.
DR   EMBL; U10400; AAB68946.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06707.1; -; Genomic_DNA.
DR   PIR; S46792; WZBYRS.
DR   RefSeq; NP_011882.1; NM_001179148.1.
DR   AlphaFoldDB; P04076; -.
DR   SMR; P04076; -.
DR   BioGRID; 36447; 33.
DR   DIP; DIP-4306N; -.
DR   FunCoup; P04076; 1418.
DR   IntAct; P04076; 4.
DR   STRING; 4932.YHR018C; -.
DR   iPTMnet; P04076; -.
DR   PaxDb; 4932-YHR018C; -.
DR   PeptideAtlas; P04076; -.
DR   TopDownProteomics; P04076; -.
DR   EnsemblFungi; YHR018C_mRNA; YHR018C; YHR018C.
DR   GeneID; 856411; -.
DR   KEGG; sce:YHR018C; -.
DR   AGR; SGD:S000001060; -.
DR   SGD; S000001060; ARG4.
DR   VEuPathDB; FungiDB:YHR018C; -.
DR   eggNOG; KOG1316; Eukaryota.
DR   HOGENOM; CLU_027272_2_1_1; -.
DR   InParanoid; P04076; -.
DR   OMA; AAAWQVM; -.
DR   OrthoDB; 2561043at2759; -.
DR   BioCyc; YEAST:YHR018C-MONOMER; -.
DR   Reactome; R-SCE-70635; Urea cycle.
DR   UniPathway; UPA00068; UER00114.
DR   BioGRID-ORCS; 856411; 10 hits in 10 CRISPR screens.
DR   CD-CODE; E03F929F; Stress granule.
DR   PRO; PR:P04076; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P04076; protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IDA:SGD.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IDA:SGD.
DR   CDD; cd01359; Argininosuccinate_lyase; 1.
DR   FunFam; 1.10.275.10:FF:000002; Argininosuccinate lyase; 1.
DR   FunFam; 1.10.40.30:FF:000001; Argininosuccinate lyase; 1.
DR   FunFam; 1.20.200.10:FF:000002; Argininosuccinate lyase; 1.
DR   Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR   HAMAP; MF_00006; Arg_succ_lyase; 1.
DR   InterPro; IPR029419; Arg_succ_lyase_C.
DR   InterPro; IPR009049; Argininosuccinate_lyase.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR022761; Fumarate-Lyase-like_N.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   NCBIfam; TIGR00838; argH; 1.
DR   PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR   Pfam; PF14698; ASL_C2; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Lyase; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..463
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000137727"
FT   ACT_SITE        162
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P24058"
FT   ACT_SITE        283
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P24058"
FT   BINDING         27
FT                   /ligand="2-(N(omega)-L-arginino)succinate"
FT                   /ligand_id="ChEBI:CHEBI:57472"
FT                   /ligand_note="ligand shared between tetrameric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000250|UniProtKB:P24058"
FT   BINDING         115
FT                   /ligand="2-(N(omega)-L-arginino)succinate"
FT                   /ligand_id="ChEBI:CHEBI:57472"
FT                   /ligand_note="ligand shared between tetrameric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000250|UniProtKB:P24058"
FT   BINDING         161
FT                   /ligand="2-(N(omega)-L-arginino)succinate"
FT                   /ligand_id="ChEBI:CHEBI:57472"
FT                   /ligand_note="ligand shared between tetrameric partners"
FT                   /note="in chain C"
FT                   /evidence="ECO:0000250|UniProtKB:P24058"
FT   BINDING         291
FT                   /ligand="2-(N(omega)-L-arginino)succinate"
FT                   /ligand_id="ChEBI:CHEBI:57472"
FT                   /ligand_note="ligand shared between tetrameric partners"
FT                   /note="in chain B"
FT                   /evidence="ECO:0000250|UniProtKB:P24058"
FT   BINDING         323
FT                   /ligand="2-(N(omega)-L-arginino)succinate"
FT                   /ligand_id="ChEBI:CHEBI:57472"
FT                   /ligand_note="ligand shared between tetrameric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000250|UniProtKB:P24058"
FT   BINDING         328
FT                   /ligand="2-(N(omega)-L-arginino)succinate"
FT                   /ligand_id="ChEBI:CHEBI:57472"
FT                   /ligand_note="ligand shared between tetrameric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000250|UniProtKB:P24058"
FT   BINDING         331
FT                   /ligand="2-(N(omega)-L-arginino)succinate"
FT                   /ligand_id="ChEBI:CHEBI:57472"
FT                   /ligand_note="ligand shared between tetrameric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000250|UniProtKB:P24058"
FT   SITE            296
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000250|UniProtKB:P24058"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        103
FT                   /note="D -> E (in Ref. 1; AAA34434)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   463 AA;  51989 MW;  2E5C01E53B3E163B CRC64;
     MSDGTQKLWG GRFTGETDPL MHLYNASLPY DYKMYKADLE GTKVYTAGLQ KLGLLTETEL
     AKIHEGLAEI KKEWDADKFV RHPNDEDIHT ANERRLGELI GRDIAGKVHT GRSRNDQVVT
     DLRIYCRDIV NDTLFPALKG LVEVLIKRAE GEIDVLMPGY THLQRAQPIR WSHWLSSYAT
     YFTEDYKRLG QILHRLNQSP LGAGALAGHP YGIDREFLAE GLGFNSVIGN SLVAVSDRDF
     IVELMFWGTL FMNHISRFAE DLIIYCTAEF GFIQLSDAYS TGSSLMPQKK NADSLELLRG
     KSGRVFGDLT GFLMSLKGIP STYDKDMQED KEPLFDCLTT VEHSMLIATG VISTLTVNKE
     KMEAALTMDM LATDLADYLV RKGVPFRETH HISGECVATA ERLGLSGIDK LTLEQYQKID
     SRFGQDLFET FNFEQSVERR DATGGTAKSA VLKQLDNLKS QLN
//