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Database: UniProt
Entry: P07244
LinkDB: P07244
Original site: P07244 
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   16-JAN-2019, entry version 186.
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:
CC       Reaction=5-phospho-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC         N(1)-(5-phospho-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58089,
CC         ChEBI:CHEBI:58457, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(formamido)-N(1)-(5-phospho-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:58478,
CC         ChEBI:CHEBI:137981, ChEBI:CHEBI:456216; EC=6.3.3.1;
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}.
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; -.
DR   BioGrid; 33005; 66.
DR   DIP; DIP-4080N; -.
DR   IntAct; P07244; 27.
DR   MINT; P07244; -.
DR   STRING; 4932.YGL234W; -.
DR   iPTMnet; P07244; -.
DR   MaxQB; P07244; -.
DR   PaxDb; P07244; -.
DR   PRIDE; P07244; -.
DR   EnsemblFungi; YGL234W_mRNA; YGL234W_mRNA; YGL234W.
DR   GeneID; 852617; -.
DR   KEGG; sce:YGL234W; -.
DR   SGD; S000003203; ADE5,7.
DR   GeneTree; ENSGT00390000000292; -.
DR   HOGENOM; HOG000030315; -.
DR   InParanoid; P07244; -.
DR   KO; K11788; -.
DR   OMA; LLERHNC; -.
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: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; 3.30.1330.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.90.600.10; -; 1.
DR   Gene3D; 3.90.650.10; -; 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   PANTHER; PTHR10520; PTHR10520; 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; SM01210; GARS_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   SUPFAM; SSF55326; SSF55326; 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
//
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