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 06-JUL-2016, entry version 164. DE RecName: Full=Bifunctional purine biosynthetic protein ADE5,7; DE Includes: DE RecName: Full=Phosphoribosylamine--glycine ligase; DE EC=6.3.4.13; DE AltName: Full=Glycinamide ribonucleotide synthetase; DE Short=GARS; DE AltName: Full=Phosphoribosylglycinamide synthetase; DE Includes: DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase; DE EC=6.3.3.1; DE AltName: Full=AIR synthase; DE Short=AIRS; DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase; GN Name=ADE5,7; OrderedLocusNames=YGL234W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; 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 RT overlapping 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., RA Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., RA Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., RA Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E., RA Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., RA Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., RA Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., RA Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., RA Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., RA Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., RA Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., RA Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., RA Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., RA Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., RA Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., RA Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., RA Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., RA Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., RA Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., RA van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., RA Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., RA Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., RA 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT 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., RA Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., RA Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., RA Kolodner R.D., LaBaer J.; RT "Approaching a complete repository of sequence-verified protein- RT encoding 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 RT of a gene-protein index."; RL Yeast 11:601-613(1995). 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., RA Dephoure N., 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-455, AND IDENTIFICATION RP BY 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 RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [8] 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 RT insights into evolution."; RL Science 325:1682-1686(2009). RN [9] 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., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP CC + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. CC -!- CATALYTIC ACTIVITY: ATP + 2-(formamido)-N(1)-(5-phospho-D- CC ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D- CC ribosyl)imidazole. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-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; CC N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D- CC ribose 1-diphosphate: step 2/2. 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 -!- SIMILARITY: Contains 1 ATP-grasp domain. {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 ProteinModelPortal; P07244; -. DR SMR; P07244; 2-439, 449-788. DR BioGrid; 33005; 37. DR DIP; DIP-4080N; -. DR IntAct; P07244; 15. DR MINT; MINT-550925; -. DR iPTMnet; P07244; -. DR MaxQB; P07244; -. DR EnsemblFungi; YGL234W; YGL234W; YGL234W. DR GeneID; 852617; -. DR KEGG; sce:YGL234W; -. DR EuPathDB; FungiDB:YGL234W; -. DR SGD; S000003203; ADE5,7. DR GeneTree; ENSGT00390000000292; -. DR HOGENOM; HOG000030315; -. DR InParanoid; P07244; -. DR KO; K11788; -. DR OMA; GMLFTGF; -. DR OrthoDB; EOG7Q8CXX; -. 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 PRO; PR:P07244; -. DR Proteomes; UP000002311; Chromosome VII. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. 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:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0006144; P:purine nucleobase metabolic process; TAS:SGD. DR Gene3D; 3.30.1330.10; -; 1. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.90.600.10; -; 1. DR Gene3D; 3.90.650.10; -; 1. DR HAMAP; MF_00138; GARS; 1. DR HAMAP; MF_00741; AIRS; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp. DR InterPro; IPR000115; PRibGlycinamide_synth. DR InterPro; IPR020560; PRibGlycinamide_synth_C-dom. DR InterPro; IPR020559; PRibGlycinamide_synth_CS. DR InterPro; IPR020562; PRibGlycinamide_synth_N. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR004733; PurM_cligase. DR InterPro; IPR011054; Rudment_hybrid_motif. 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; SM01210; GARS_C; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR SUPFAM; SSF56042; SSF56042; 1. DR TIGRFAMs; TIGR00877; purD; 1. DR TIGRFAMs; TIGR00878; purM; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00184; GARS; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Direct protein sequencing; Ligase; KW Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding; KW Phosphoprotein; Purine biosynthesis; Reference proteome. FT CHAIN 1 802 Bifunctional purine biosynthetic protein FT ADE5,7. FT /FTId=PRO_0000074941. FT DOMAIN 114 330 ATP-grasp. FT NP_BIND 140 203 ATP. {ECO:0000250}. FT REGION 1 450 GARS. FT REGION 451 802 AIRS. FT METAL 298 298 Manganese. {ECO:0000250}. FT METAL 300 300 Manganese. {ECO:0000250}. FT MOD_RES 455 455 Phosphoserine. FT {ECO:0000244|PubMed:18407956, FT ECO:0000244|PubMed:19779198}. FT MOD_RES 458 458 Phosphoserine. FT {ECO:0000244|PubMed:19779198}. FT CONFLICT 28 28 K -> R (in Ref. 4; AAT93005). FT {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 //