PUR7_YEAST
ID PUR7_YEAST Reviewed; 306 AA.
AC P27616; D6VPM4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase;
DE EC=6.3.2.6 {ECO:0000269|PubMed:1756975};
DE AltName: Full=SAICAR synthetase;
GN Name=ADE1; OrderedLocusNames=YAR015W;
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=3013210;
RA Myasnikov A.N., Plavnik Y.A., Sasnauskas K.V., Gedminene G.K.,
RA Yanulaitis A.A., Smirnov M.N.;
RT "Nucleotide sequence of the ADE1 gene of the yeast Saccharomyces
RT cerevisiae.";
RL Bioorg. Khim. 12:555-558(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1756975; DOI=10.1016/0378-1119(91)90600-g;
RA Myasnikov A.N., Sasnauskas K.V., Janulaitis A.A., Smirnov M.N.;
RT "The Saccharomyces cerevisiae ADE1 gene: structure, overexpression and
RT possible regulation by general amino acid control.";
RL Gene 109:143-147(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1658741; DOI=10.1093/nar/19.20.5731;
RA Davies C.J., Hutchison C.A. III;
RT "A directed DNA sequencing strategy based upon Tn3 transposon mutagenesis:
RT application to the ADE1 locus on Saccharomyces cerevisiae chromosome I.";
RL Nucleic Acids Res. 19:5731-5738(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=7941740; DOI=10.1002/yea.320100413;
RA Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
RA Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42
RT kbp SPO7-CENI-CDC15 region.";
RL Yeast 10:535-541(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 285-306.
RX PubMed=1495480; DOI=10.1007/bf00272358;
RA Schweitzer B., Philippsen P.;
RT "NPK1, a nonessential protein kinase gene in Saccharomyces cerevisiae with
RT similarity to Aspergillus nidulans nimA.";
RL Mol. Gen. Genet. 234:164-167(1992).
RN [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND ACETYLATION AT SER-2.
RX PubMed=9551557; DOI=10.1016/s0969-2126(98)00038-0;
RA Levdikov V.M., Barynin V.V., Grebenko A.I., Melik-Adamyan W.R.,
RA Lamzin V.S., Wilson K.S.;
RT "The structure of SAICAR synthase: an enzyme in the de novo pathway of
RT purine nucleotide biosynthesis.";
RL Structure 6:363-376(1998).
CC -!- FUNCTION: Catalyzes the reaction of 4-carboxy-5-aminoimidazole ribotide
CC (CAIR) and aspartic acid with the formation of N-succinyl-5-amino-
CC imidazole-4-carboxamide ribotide (SAICAR) in the purine biosynthesis
CC pathway. {ECO:0000269|PubMed:1756975}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP +
CC L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-
CC 4-carboxamido]succinate + ADP + 2 H(+) + phosphate;
CC Xref=Rhea:RHEA:22628, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58443,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:456216; EC=6.3.2.6;
CC Evidence={ECO:0000269|PubMed:1756975};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22629;
CC Evidence={ECO:0000305|PubMed:1756975};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC {ECO:0000305|PubMed:1756975}.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P27616; P02829: HSP82; NbExp=2; IntAct=EBI-14257, EBI-8659;
CC -!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SAICAR synthetase family. {ECO:0000305}.
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DR EMBL; M61209; AAA34396.1; -; Genomic_DNA.
DR EMBL; M67445; AAA34398.1; -; Genomic_DNA.
DR EMBL; L22015; AAC04963.1; -; Genomic_DNA.
DR EMBL; X60549; CAA43043.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06994.1; -; Genomic_DNA.
DR PIR; S20122; JQ1395.
DR RefSeq; NP_009409.1; NM_001178216.1.
DR PDB; 1A48; X-ray; 1.90 A; A=2-306.
DR PDB; 1OBD; X-ray; 1.40 A; A=2-306.
DR PDB; 1OBG; X-ray; 2.05 A; A=2-306.
DR PDB; 2CNQ; X-ray; 1.00 A; A=2-306.
DR PDB; 2CNU; X-ray; 1.05 A; A=2-306.
DR PDB; 2CNV; X-ray; 2.00 A; A=2-306.
DR PDBsum; 1A48; -.
DR PDBsum; 1OBD; -.
DR PDBsum; 1OBG; -.
DR PDBsum; 2CNQ; -.
DR PDBsum; 2CNU; -.
DR PDBsum; 2CNV; -.
DR AlphaFoldDB; P27616; -.
DR SMR; P27616; -.
DR BioGRID; 31799; 66.
DR IntAct; P27616; 2.
DR MINT; P27616; -.
DR STRING; 4932.YAR015W; -.
DR iPTMnet; P27616; -.
DR SWISS-2DPAGE; P27616; -.
DR MaxQB; P27616; -.
DR PaxDb; P27616; -.
DR PRIDE; P27616; -.
DR EnsemblFungi; YAR015W_mRNA; YAR015W; YAR015W.
DR GeneID; 851272; -.
DR KEGG; sce:YAR015W; -.
DR SGD; S000000070; ADE1.
DR VEuPathDB; FungiDB:YAR015W; -.
DR eggNOG; KOG2835; Eukaryota.
DR GeneTree; ENSGT00390000010172; -.
DR HOGENOM; CLU_045637_0_2_1; -.
DR InParanoid; P27616; -.
DR OMA; TKFEFGF; -.
DR BioCyc; MetaCyc:YAR015W-MON; -.
DR BioCyc; YEAST:YAR015W-MON; -.
DR BRENDA; 6.3.2.6; 984.
DR UniPathway; UPA00074; UER00131.
DR EvolutionaryTrace; P27616; -.
DR PRO; PR:P27616; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P27616; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IDA:SGD.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IDA:SGD.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IDA:SGD.
DR HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR001636; SAICAR_synth.
DR InterPro; IPR018236; SAICAR_synthetase_CS.
DR Pfam; PF01259; SAICAR_synt; 1.
DR TIGRFAMs; TIGR00081; purC; 1.
DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Ligase; Nucleotide-binding;
KW Purine biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9551557,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..306
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_0000100929"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9551557,
FT ECO:0007744|PubMed:22814378"
FT CONFLICT 185
FT /note="E -> G (in Ref. 1; AAA34396 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:2CNQ"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:2CNQ"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:2CNQ"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:2CNQ"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:2CNQ"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:2CNQ"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:2CNQ"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:2CNQ"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:2CNQ"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:2CNQ"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:2CNQ"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:2CNQ"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2CNQ"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:2CNQ"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:2CNQ"
FT HELIX 185..209
FT /evidence="ECO:0007829|PDB:2CNQ"
FT STRAND 211..223
FT /evidence="ECO:0007829|PDB:2CNQ"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:2CNQ"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:2CNQ"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:2CNQ"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:2CNQ"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:2CNQ"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:2CNU"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:2CNQ"
FT HELIX 282..300
FT /evidence="ECO:0007829|PDB:2CNQ"
SQ SEQUENCE 306 AA; 34603 MW; A9AF2D450F25862A CRC64;
MSITKTELDG ILPLVARGKV RDIYEVDAGT LLFVATDRIS AYDVIMENSI PEKGILLTKL
SEFWFKFLSN DVRNHLVDIA PGKTIFDYLP AKLSEPKYKT QLEDRSLLVH KHKLIPLEVI
VRGYITGSAW KEYVKTGTVH GLKQPQGLKE SQEFPEPIFT PSTKAEQGEH DENISPAQAA
ELVGEDLSRR VAELAVKLYS KCKDYAKEKG IIIADTKFEF GIDEKTNEII LVDEVLTPDS
SRFWNGASYK VGESQDSYDK QFLRDWLTAN KLNGVNGVKM PQDIVDRTRA KYIEAYETLT
GSKWSH
