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 27-MAR-2024, entry version 202. 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}. 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; 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; 67. DR IntAct; P27616; 2. DR MINT; P27616; -. DR STRING; 4932.YAR015W; -. DR iPTMnet; P27616; -. DR MaxQB; P27616; -. DR PaxDb; 4932-YAR015W; -. DR PeptideAtlas; P27616; -. DR EnsemblFungi; YAR015W_mRNA; YAR015W; YAR015W. DR GeneID; 851272; -. DR KEGG; sce:YAR015W; -. DR AGR; SGD:S000000070; -. 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; CEPFKVE; -. DR OrthoDB; 605at2759; -. DR BioCyc; MetaCyc:YAR015W-MONOMER; -. DR BioCyc; YEAST:YAR015W-MONOMER; -. DR BRENDA; 6.3.2.6; 984. DR UniPathway; UPA00074; UER00131. DR BioGRID-ORCS; 851272; 5 hits in 10 CRISPR screens. 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 CDD; cd01414; SAICAR_synt_Sc; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. 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 NCBIfam; TIGR00081; purC; 1. DR PANTHER; PTHR43700; PHOSPHORIBOSYLAMINOIMIDAZOLE-SUCCINOCARBOXAMIDE SYNTHASE; 1. DR PANTHER; PTHR43700:SF1; PHOSPHORIBOSYLAMINOIMIDAZOLE-SUCCINOCARBOXAMIDE SYNTHASE; 1. DR Pfam; PF01259; SAICAR_synt; 1. DR SUPFAM; SSF56104; SAICAR synthase-like; 1. DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1. DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1. DR SWISS-2DPAGE; P27616; -. 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 //