GCH1_YEAST
ID GCH1_YEAST Reviewed; 243 AA.
AC P51601; D6VV45;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=GTP cyclohydrolase 1 {ECO:0000303|Ref.1};
DE EC=3.5.4.16 {ECO:0000305|Ref.1};
DE AltName: Full=GTP cyclohydrolase I {ECO:0000303|Ref.1};
DE Short=GTP-CH-I {ECO:0000303|Ref.1};
GN Name=FOL2 {ECO:0000303|Ref.1}; OrderedLocusNames=YGR267C; ORFNames=G9349;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=C836;
RA Witter K., Guetlich M., Stucka R., Ziegler I., Bacher A.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8573145; DOI=10.1006/bbrc.1996.0048;
RA Nardese V., Gutlich M., Brambilla A., Agostoni Carbone M.L.;
RT "Disruption of the GTP-cyclohydrolase I gene in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 218:273-279(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9605509;
RX DOI=10.1002/(sici)1097-0061(19980430)14:6<587::aid-yea268>3.0.co;2-i;
RA Agostoni Carbone M.L., Lucchini G., Melchioretto P., Nardese V., Vanoni M.,
RA Panzeri L.;
RT "A 9359 bp fragment from the right arm of Saccharomyces cerevisiae
RT chromosome VII includes the FOL2 and YTA7 genes and three unknown open
RT reading frames.";
RL Yeast 14:587-591(1998).
RN [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 115-208.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7542887; DOI=10.1006/bbrc.1995.2026;
RA Maier J., Witter K., Guetlich M., Ziegler I., Werner T., Ninnemann H.;
RT "Homology cloning of GTP-cyclohydrolase I from various unrelated eukaryotes
RT by reverse-transcription polymerase chain reaction using a general set of
RT degenerate primers.";
RL Biochem. Biophys. Res. Commun. 212:705-711(1995).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-23, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-23, 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 [12]
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: GTP cyclohydrolase 1 is the first enzyme in the biosynthetic
CC pathway leading to folic acid. {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate +
CC H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:58462; EC=3.5.4.16;
CC Evidence={ECO:0000305|Ref.1};
CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC {ECO:0000305|Ref.1}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8VYU3}.
CC -!- DISRUPTION PHENOTYPE: Leads to folinic acid auxotrophy, and lacks any
CC detectable specific enzymatic activity. {ECO:0000269|Ref.1}.
CC -!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. {ECO:0000305}.
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DR EMBL; Z47201; CAA87397.1; -; Genomic_DNA.
DR EMBL; X94314; CAA63975.1; -; Genomic_DNA.
DR EMBL; Y07893; CAA69198.1; -; Genomic_DNA.
DR EMBL; Z73052; CAA97297.1; -; Genomic_DNA.
DR EMBL; AY692993; AAT93012.1; -; Genomic_DNA.
DR EMBL; Z49756; CAA89826.1; -; mRNA.
DR EMBL; BK006941; DAA08356.1; -; Genomic_DNA.
DR PIR; JC4585; JC4585.
DR RefSeq; NP_011783.1; NM_001181396.1.
DR AlphaFoldDB; P51601; -.
DR SMR; P51601; -.
DR BioGRID; 33517; 49.
DR DIP; DIP-1318N; -.
DR IntAct; P51601; 15.
DR MINT; P51601; -.
DR STRING; 4932.YGR267C; -.
DR iPTMnet; P51601; -.
DR MaxQB; P51601; -.
DR PaxDb; P51601; -.
DR PRIDE; P51601; -.
DR EnsemblFungi; YGR267C_mRNA; YGR267C; YGR267C.
DR GeneID; 853183; -.
DR KEGG; sce:YGR267C; -.
DR SGD; S000003499; FOL2.
DR VEuPathDB; FungiDB:YGR267C; -.
DR eggNOG; KOG2698; Eukaryota.
DR GeneTree; ENSGT00390000013481; -.
DR HOGENOM; CLU_049768_1_3_1; -.
DR InParanoid; P51601; -.
DR OMA; CEHMCMS; -.
DR BioCyc; YEAST:YGR267C-MON; -.
DR Reactome; R-SCE-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR UniPathway; UPA00848; UER00151.
DR PRO; PR:P51601; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P51601; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IMP:SGD.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IMP:SGD.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IBA:GO_Central.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.286.10; -; 1.
DR Gene3D; 3.30.1130.10; -; 1.
DR HAMAP; MF_00223; FolE; 1.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR InterPro; IPR043134; GTP-CH-I_N.
DR InterPro; IPR001474; GTP_CycHdrlase_I.
DR InterPro; IPR018234; GTP_CycHdrlase_I_CS.
DR InterPro; IPR020602; GTP_CycHdrlase_I_dom.
DR PANTHER; PTHR11109; PTHR11109; 1.
DR Pfam; PF01227; GTP_cyclohydroI; 1.
DR TIGRFAMs; TIGR00063; folE; 1.
DR PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
DR PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Folate biosynthesis; GTP-binding; Hydrolase;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Zinc.
FT CHAIN 1..243
FT /note="GTP cyclohydrolase 1"
FT /id="PRO_0000119489"
FT REGION 18..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30793"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30793"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30793"
FT MOD_RES 15
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 159..160
FT /note="LA -> QG (in Ref. 7; CAA89826)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="S -> M (in Ref. 7; CAA89826)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="V -> A (in Ref. 1; CAA87397)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 243 AA; 27769 MW; A71AB8750AECD3F6 CRC64;
MHNIQLVQEI ERHETPLNIR PTSPYTLNPP VERDGFSWPS VGTRQRAEET EEEEKERIQR
ISGAIKTILT ELGEDVNREG LLDTPQRYAK AMLYFTKGYQ TNIMDDVIKN AVFEEDHDEM
VIVRDIEIYS LCEHHLVPFF GKVHIGYIPN KKVIGLSKLA RLAEMYARRL QVQERLTKQI
AMALSDILKP LGVAVVMEAS HMCMVSRGIQ KTGSSTVTSC MLGGFRAHKT REEFLTLLGR
RSI
