ARLY_YEAST
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 03-AUG-2022, entry version 196.
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; 21.
DR DIP; DIP-4306N; -.
DR IntAct; P04076; 3.
DR STRING; 4932.YHR018C; -.
DR iPTMnet; P04076; -.
DR MaxQB; P04076; -.
DR PaxDb; P04076; -.
DR PRIDE; P04076; -.
DR TopDownProteomics; P04076; -.
DR EnsemblFungi; YHR018C_mRNA; YHR018C; YHR018C.
DR GeneID; 856411; -.
DR KEGG; sce:YHR018C; -.
DR SGD; S000001060; ARG4.
DR VEuPathDB; FungiDB:YHR018C; -.
DR eggNOG; KOG1316; Eukaryota.
DR GeneTree; ENSGT00950000183122; -.
DR HOGENOM; CLU_027272_2_1_1; -.
DR InParanoid; P04076; -.
DR OMA; KKNPDVF; -.
DR BioCyc; YEAST:YHR018C-MON; -.
DR Reactome; R-SCE-70635; Urea cycle.
DR UniPathway; UPA00068; UER00114.
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:0042450; P:arginine biosynthetic process via ornithine; IDA:SGD.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR Gene3D; 1.10.275.10; -; 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; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR PANTHER; PTHR43814; PTHR43814; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00838; argH; 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
