PUR4_YEAST
ID PUR4_YEAST Reviewed; 1358 AA.
AC P38972; D6VUJ6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase;
DE Short=FGAM synthase;
DE Short=FGAMS;
DE EC=6.3.5.3;
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase;
DE Short=FGAR amidotransferase;
DE Short=FGAR-AT;
DE AltName: Full=Formylglycinamide ribotide amidotransferase;
GN Name=ADE6; OrderedLocusNames=YGR061C;
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].
RA Andreichuk Y.V., Domkin V.D.;
RT "Saccharomyces cerevisiae formylglycinamide ribonucleotide synthetase.";
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
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 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 [5]
RP IDENTIFICATION 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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Phosphoribosylformylglycinamidine synthase involved in the
CC purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of
CC formylglycinamide ribonucleotide (FGAR) and glutamine to yield
CC formylglycinamidine ribonucleotide (FGAM) and glutamate (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC ChEBI:CHEBI:456216; EC=6.3.5.3;
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 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Present with 40800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000305}.
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DR EMBL; U14566; AAA50357.1; -; Genomic_DNA.
DR EMBL; Z72846; CAA97063.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08157.1; -; Genomic_DNA.
DR PIR; S64356; S64356.
DR RefSeq; NP_011575.1; NM_001181190.1.
DR AlphaFoldDB; P38972; -.
DR SMR; P38972; -.
DR BioGRID; 33306; 119.
DR DIP; DIP-1175N; -.
DR IntAct; P38972; 5.
DR MINT; P38972; -.
DR STRING; 4932.YGR061C; -.
DR iPTMnet; P38972; -.
DR MaxQB; P38972; -.
DR PaxDb; P38972; -.
DR PRIDE; P38972; -.
DR EnsemblFungi; YGR061C_mRNA; YGR061C; YGR061C.
DR GeneID; 852952; -.
DR KEGG; sce:YGR061C; -.
DR SGD; S000003293; ADE6.
DR VEuPathDB; FungiDB:YGR061C; -.
DR eggNOG; KOG1907; Eukaryota.
DR GeneTree; ENSGT00390000007600; -.
DR HOGENOM; CLU_001031_0_2_1; -.
DR InParanoid; P38972; -.
DR OMA; LSANWMW; -.
DR BioCyc; MetaCyc:YGR061C-MON; -.
DR BioCyc; YEAST:YGR061C-MON; -.
DR Reactome; R-SCE-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00128.
DR PRO; PR:P38972; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P38972; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IMP:SGD.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IC:SGD.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:SGD.
DR Gene3D; 3.30.1330.10; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.650.10; -; 2.
DR HAMAP; MF_00419; PurL_1; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR040707; FGAR-AT_N.
DR InterPro; IPR010073; PurL_large.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR036604; PurS-like_sf.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF55326; SSF55326; 2.
DR SUPFAM; SSF56042; SSF56042; 2.
DR SUPFAM; SSF82697; SSF82697; 1.
DR TIGRFAMs; TIGR01735; FGAM_synt; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Glutamine amidotransferase; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1358
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100405"
FT DOMAIN 1093..1358
FT /note="Glutamine amidotransferase type-1"
FT REGION 339..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1187
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 1319
FT /evidence="ECO:0000250"
FT ACT_SITE 1321
FT /evidence="ECO:0000250"
FT BINDING 345..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 424..426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 719
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 720
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 762
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 766
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 930
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 932
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CONFLICT 84
FT /note="A -> L (in Ref. 1; AAA50357)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..220
FT /note="DS -> EC (in Ref. 1; AAA50357)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="L -> V (in Ref. 1; AAA50357)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="A -> P (in Ref. 1; AAA50357)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="G -> R (in Ref. 1; AAA50357)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="A -> T (in Ref. 1; AAA50357)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="E -> K (in Ref. 1; AAA50357)"
FT /evidence="ECO:0000305"
FT CONFLICT 1169..1170
FT /note="SQ -> TSSK (in Ref. 1; AAA50357)"
FT /evidence="ECO:0000305"
FT CONFLICT 1298
FT /note="G -> A (in Ref. 1; AAA50357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1358 AA; 148905 MW; A48A24ECB1BE7973 CRC64;
MTDYILPGPK ALSQFRVDNL IKDINSYTNS TSVINELRSC YIHYVNGIAQ NLSEQDTKLL
EVLLTYDSAL DIANDPLARQ LNDAVANNLP SSALGEDTYL IRVVPRSGTI SPWSSKATNI
AHVCGLQDKV QRIERGLALL IKTVPGFPLL ENLNDISLKC VYDRMTQQLY LTEPPNTMSI
FTHEEPKPLV HVPLTPKDTK QSPKDILSKA NTELGLALDS GEMEYLIHAF VETMKRDPTD
VELFMFAQVN SEHCRHKIFN ADWTIDGIKQ QFTLFQMIRN THKLNPEYTI SAYSDNAAVL
DSENDAFFFA PNSTTKEWTS TKERIPLLIK VETHNHPTAV SPFPGAATGS GGEIRDEGAT
GRGSKTKCGL SGFSVSDLLI PGNEQPWELN IGKPYHIASA LDIMIEAPLG SAAFNNEFGR
PCINGYFRTL TTKVLNHQGK EEIRGFHKPI MIAGGFGTVR PQFALKNTPI TPGSCLIVLG
GQSMLIGLGG GAASSVASGE GSADLDFASV QRGNPEMERR CQQVIDACVA LGNNNPIQSI
HDVGAGGLSN ALPELVHDND LGAKFDIRKV LSLEPGMSPM EIWCNESQER YVLGVSPQDL
SIFEEICKRE RAPFAVVGHA TAEQKLIVED PLLKTTPIDL EMPILFGKPP KMSRETITEA
LNLPEANLSE IPSLQDAIQR VLNLPSVGSK SFLITIGDRS VTGLIDRDQF VGPWQVPVAD
VGVTGTSLGE TIISTGEAMA MGEKPVNALI SASASAKLSV AESLLNIFAA DVKSLNHIKL
SANWMSPASH QGEGSKLYEA VQALGLDLCP ALGVAIPVGK DSMSMKMKWD DKEVTAPLSL
NITAFAPVFN TSKTWTPLLN RNTDDSVLVL VDLSAKQETK SLGASALLQV YNQVGNKSPT
VYDNAILKGF LESLIQLHQQ KEDIVLAYHD RSDGGLLITL LEMAFASRCG LEINIDGGDL
ESQLTNLFNE ELGAVFQISA KNLSKFEKIL NENGVAKEYI SIVGKPSFQS QEIKIINSTT
NDVIYANSRS ELEQTWSKTS YEMQKLRDNP KTAEEEFASI TDDRDPGLQY ALTYNPADDM
KIGLELSSQR PKVAILREQG VNGQMEMAWC FQQAGFNSVD VTMTDLLEGR FHLDDFIGLA
ACGGFSYGDV LGAGAGWAKS VLYHEGVRSQ FSKFFNERQD TFAFGACNGC QFLSRLKDII
PGCENWPSFE RNVSEQYEAR VCMVQISQEK DNSSEESVFL NGMAGSKLPI AVAHGEGKAT
FSKSAEQLEK FEKDGLCCIR YVDNYGNVTE RFPFNPNGST NGIAGIKSPN GRVLAMMPHP
ERVCRLEANS WYPEGKYEEW GGYGPWIRLF RSARRWVG
