ID PUR2_YEAST Reviewed; 802 AA. AC P07244; D6VVA0; E9P907; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 29-MAY-2024, entry version 213. DE RecName: Full=Bifunctional purine biosynthetic protein ADE5,7; DE Includes: DE RecName: Full=Phosphoribosylamine--glycine ligase; DE EC=6.3.4.13 {ECO:0000250|UniProtKB:P20772}; DE AltName: Full=Glycinamide ribonucleotide synthetase; DE Short=GAR synthetase {ECO:0000305}; DE Short=GARS; DE AltName: Full=Phosphoribosylglycinamide synthetase; DE Includes: DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase; DE EC=6.3.3.1 {ECO:0000250|UniProtKB:P20772}; DE AltName: Full=AIR synthase; DE Short=AIR synthetase; DE Short=AIRS; DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase; GN Name=ADE57 {ECO:0000312|SGD:S000003203}; GN Synonyms=ADE5,7 {ECO:0000303|PubMed:3097325}; GN OrderedLocusNames=YGL234W {ECO:0000312|SGD:S000003203}; 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=3097325; DOI=10.1016/0022-2836(86)90238-x; RA Henikoff S.; RT "The Saccharomyces cerevisiae ADE5,7 protein is homologous to overlapping RT Drosophila melanogaster Gart polypeptides."; RL J. Mol. Biol. 190:519-528(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). 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 PROTEIN SEQUENCE OF 1-13. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7483834; DOI=10.1002/yea.320110702; RA Boucherie H., Dujardin G., Kermorgant M., Monribot C., Slonimski P.P., RA Perrot M.; RT "Two-dimensional protein map of Saccharomyces cerevisiae: construction of a RT gene-protein index."; RL Yeast 11:601-613(1995). RN [6] 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 [7] 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, 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). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-458, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [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). CC -!- FUNCTION: Catalyzes the second and fifth step in the 'de novo' purine CC biosynthesis pathway; contains phosphoribosylamine--glycine ligase CC (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS) CC activities. {ECO:0000250|UniProtKB:P20772}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + CC N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate; CC Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681, CC ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13; CC Evidence={ECO:0000250|UniProtKB:P20772}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + CC phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, CC ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1; CC Evidence={ECO:0000250|UniProtKB:P20772}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; CC Note=Binds two magnesium or manganese ions per subunit. {ECO:0000305}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5- CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 2/2. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)- CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1- CC diphosphate: step 2/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 35800 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: In the N-terminal section; belongs to the GARS family. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the AIR synthase CC 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; X04337; CAA27867.1; -; Genomic_DNA. DR EMBL; Z72756; CAA96952.1; -; Genomic_DNA. DR EMBL; AY692986; AAT93005.1; -; Genomic_DNA. DR EMBL; BK006941; DAA07884.1; -; Genomic_DNA. DR PIR; A26343; A26343. DR RefSeq; NP_011280.1; NM_001181100.1. DR AlphaFoldDB; P07244; -. DR SMR; P07244; -. DR BioGRID; 33005; 96. DR DIP; DIP-4080N; -. DR IntAct; P07244; 27. DR MINT; P07244; -. DR STRING; 4932.YGL234W; -. DR iPTMnet; P07244; -. DR MaxQB; P07244; -. DR PaxDb; 4932-YGL234W; -. DR PeptideAtlas; P07244; -. DR EnsemblFungi; YGL234W_mRNA; YGL234W; YGL234W. DR GeneID; 852617; -. DR KEGG; sce:YGL234W; -. DR AGR; SGD:S000003203; -. DR SGD; S000003203; ADE5,7. DR VEuPathDB; FungiDB:YGL234W; -. DR eggNOG; KOG0237; Eukaryota. DR GeneTree; ENSGT00390000000292; -. DR HOGENOM; CLU_005361_1_0_1; -. DR InParanoid; P07244; -. DR OMA; EVMQACC; -. DR OrthoDB; 729at2759; -. DR BioCyc; MetaCyc:YGL234W-MONOMER; -. DR BioCyc; YEAST:YGL234W-MONOMER; -. DR Reactome; R-SCE-73817; Purine ribonucleoside monophosphate biosynthesis. DR UniPathway; UPA00074; UER00125. DR UniPathway; UPA00074; UER00129. DR BioGRID-ORCS; 852617; 2 hits in 10 CRISPR screens. DR PRO; PR:P07244; -. DR Proteomes; UP000002311; Chromosome VII. DR RNAct; P07244; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; ISS:SGD. DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; ISS:SGD. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central. DR GO; GO:0006144; P:purine nucleobase metabolic process; TAS:SGD. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central. DR CDD; cd02196; PurM; 1. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal domain; 1. DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1. DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1. DR HAMAP; MF_00741; AIRS; 1. DR HAMAP; MF_00138; GARS; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp. DR InterPro; IPR000115; PRibGlycinamide_synth. DR InterPro; IPR020560; PRibGlycinamide_synth_C-dom. DR InterPro; IPR037123; PRibGlycinamide_synth_C_sf. DR InterPro; IPR020559; PRibGlycinamide_synth_CS. DR InterPro; IPR020562; PRibGlycinamide_synth_N. DR InterPro; IPR010918; PurM-like_C_dom. DR InterPro; IPR036676; PurM-like_C_sf. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR036921; PurM-like_N_sf. DR InterPro; IPR004733; PurM_cligase. DR InterPro; IPR011054; Rudment_hybrid_motif. DR NCBIfam; TIGR00877; purD; 1. DR NCBIfam; TIGR00878; purM; 1. DR PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1. DR PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR Pfam; PF01071; GARS_A; 1. DR Pfam; PF02843; GARS_C; 1. DR Pfam; PF02844; GARS_N; 1. DR SMART; SM01209; GARS_A; 1. DR SMART; SM01210; GARS_C; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 1. DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1. DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1. DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00184; GARS; 1. PE 1: Evidence at protein level; KW ATP-binding; Cytoplasm; Direct protein sequencing; Ligase; Magnesium; KW Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding; KW Phosphoprotein; Purine biosynthesis; Reference proteome. FT CHAIN 1..802 FT /note="Bifunctional purine biosynthetic protein ADE5,7" FT /id="PRO_0000074941" FT DOMAIN 114..330 FT /note="ATP-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT REGION 1..450 FT /note="GARS" FT /evidence="ECO:0000255" FT REGION 451..802 FT /note="AIRS" FT /evidence="ECO:0000255" FT BINDING 141..203 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 298 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 300 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT MOD_RES 455 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 458 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT CONFLICT 28 FT /note="K -> R (in Ref. 4; AAT93005)" FT /evidence="ECO:0000305" SQ SEQUENCE 802 AA; 86068 MW; 1583C6F3E64085D2 CRC64; MLNILVLGNG AREHVLVTKL AQSPTVGKIY VAPGNGGTAT MDPSRVINWD ITPDVANFAR LQSMAVEHKI NLVVPGPELP LVNGITSVFH SVGIPVFGPS VKAAQLEASK AFSKRFMSKH NIPTASYDVF TNPEEAISFL QAHTDKAFVI KADGIAAGKG VIIPSSIDES VQAIKDIMVT KQFGEEAGKQ VVIEQFLEGD EISLLTIVDG YSHFNLPVAQ DHKRIFDGDK GLNTGGMGAY APAPVATPSL LKTIDSQIVK PTIDGMRRDG MPFVGVLFTG MILVKDSKTN QLVPEVLEYN VRFGDPETQA VLSLLDDQTD LAQVFLAAAE HRLDSVNIGI DDTRSAVTVV VAAGGYPESY AKGDKITLDT DKLPPHTQIF QAGTKYDSAT DSLLTNGGRV LSVTSTAQDL RTAVDTVYEA VKCVHFQNSY YRKDIAYRAF QNSESSKVAI TYADSGVSVD NGNNLVQTIK EMVRSTRRPG ADSDIGGFGG LFDLAQAGFR QNEDTLLVGA TDGVGTKLII AQETGIHNTV GIDLVAMNVN DLVVQGAEPL FFLDYFATGA LDIQVASDFV SGVANGCIQS GCALVGGETS EMPGMYPPGH YDTNGTAVGA VLRQDILPKI NEMAAGDVLL GLASSGVHSN GFSLVRKIIQ HVALPWDAPC PWDESKTLGE GILEPTKIYV KQLLPSIRQR LLLGLAHITG GGLVENIPRA IPDHLQARVD MSTWEVPRVF KWFGQAGNVP HDDILRTFNM GVGMVLIVKR ENVKAVCDSL TEEGEIIWEL GSLQERPKDA PGCVIENGTK LY //