PUR2_YEAST
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 03-AUG-2022, entry version 205.
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; 82.
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; YGL234W.
DR GeneID; 852617; -.
DR KEGG; sce:YGL234W; -.
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 BioCyc; MetaCyc:YGL234W-MON; -.
DR BioCyc; YEAST:YGL234W-MON; -.
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 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; 3.30.1330.10; -; 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; 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
