ID PUR2_YEAST STANDARD; PRT; 802 AA. AC P07244; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 24-JAN-2006 (Rel. 49, Last annotation update) DE Bifunctional purine biosynthetic protein ADE5,7 [Includes: DE Phosphoribosylamine--glycine ligase (EC 6.3.4.13) (GARS) (Glycinamide DE ribonucleotide synthetase) (Phosphoribosylglycinamide synthetase); DE Phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) (AIRS) DE (Phosphoribosyl-aminoimidazole synthetase) (AIR synthase)]. GN Name=ADE5,7; OrderedLocusNames=YGL234W; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=87061006; PubMed=3097325; 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=S288c / FY1679; RX MEDLINE=97313265; 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 PARTIAL PROTEIN SEQUENCE OF 1-13. RC STRAIN=S288c; RX MEDLINE=96093904; PubMed=7483834; 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 [4] RP LEVEL OF PROTEIN EXPRESSION. RX MEDLINE=22923965; 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). 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: Nucleotide biosynthesis; IMP biosynthesis; 5-amino-1-(5- CC phospho-D-ribosyl)imidazole-4-carboxamide from N(2)-formyl-N(1)- CC (5-phospho-D-ribosyl)glycinamide: step 2. CC -!- PATHWAY: Nucleotide biosynthesis; IMP biosynthesis; N(1)-(5- CC phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1- CC diphosphate: step 2. CC -!- PATHWAY: Context: Purine biosynthesis. CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-323, EBI-323; CC -!- MISCELLANEOUS: Present with 35800 molecules/cell. CC -!- SIMILARITY: In the N-terminal section; belongs to the GARS family. CC -!- SIMILARITY: In the C-terminal section; belongs to the AIR synthase CC family. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. 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 PIR; A26343; A26343. DR HSSP; P08178; 1CLI. DR IntAct; P07244; -. DR GermOnline; 141283; -. DR Ensembl; YGL234W; Saccharomyces cerevisiae. DR SGD; S000003203; ADE5,7. DR LinkHub; P07244; -. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0042802; F:protein self binding; IPI. DR GO; GO:0006144; P:purine base metabolism; TAS. DR InterPro; IPR000728; AIR_synth. DR InterPro; IPR010918; AIR_synth_C. DR InterPro; IPR011761; ATP_GRASP. DR InterPro; IPR000115; Gars. DR InterPro; IPR004733; PurM_cligase. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR Pfam; PF01071; GARS_A; 1. DR Pfam; PF02842; GARS_B; 1. DR Pfam; PF02843; GARS_C; 1. DR Pfam; PF02844; GARS_N; 1. DR TIGRFAMs; TIGR00877; purD; 1. DR TIGRFAMs; TIGR00878; purM; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00184; GARS; 1. KW Complete proteome; Direct protein sequencing; Ligase; KW Multifunctional enzyme; Purine biosynthesis. FT DOMAIN 114 330 ATP-grasp. FT REGION 1 450 GARS. FT REGION 451 802 AIRS. 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 //