RIB1_YEAST
ID RIB1_YEAST Reviewed; 345 AA.
AC P38066; D6VPW6;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=GTP cyclohydrolase-2;
DE EC=3.5.4.25;
DE AltName: Full=GTP cyclohydrolase II;
GN Name=RIB1; OrderedLocusNames=YBL033C; ORFNames=YBL0417;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091857; DOI=10.1002/yea.320100003;
RA Skala J., van Dyck L., Purnelle B., Goffeau A.;
RT "The sequence of an 8.8 kb segment on the left arm of chromosome II from
RT Saccharomyces cerevisiae reveals four new open reading frames including
RT homologs of animal DNA polymerase alpha-primases and bacterial GTP
RT cyclohydrolase II.";
RL Yeast 10:S13-S24(1994).
RN [2]
RP SEQUENCE REVISION TO 181.
RA Skala J., van Dyck L., Purnelle B., Goffeau A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
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 [5]
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).
CC -!- FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6-
CC ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and
CC pyrophosphate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-
CC pyrimidine + formate + 3 H(+) + 2 phosphate; Xref=Rhea:RHEA:23704,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58614; EC=3.5.4.25;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC ribitylamino)uracil from GTP: step 1/4.
CC -!- MISCELLANEOUS: Present with 9520 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase II 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; Z35794; CAA84853.1; -; Genomic_DNA.
DR EMBL; X74738; CAA52759.1; -; Genomic_DNA.
DR EMBL; Z21617; CAA79741.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07086.1; -; Genomic_DNA.
DR PIR; S45767; S45767.
DR RefSeq; NP_009520.1; NM_001178273.1.
DR AlphaFoldDB; P38066; -.
DR SMR; P38066; -.
DR BioGRID; 32664; 14.
DR DIP; DIP-3936N; -.
DR IntAct; P38066; 6.
DR MINT; P38066; -.
DR STRING; 4932.YBL033C; -.
DR iPTMnet; P38066; -.
DR MaxQB; P38066; -.
DR PaxDb; P38066; -.
DR PRIDE; P38066; -.
DR EnsemblFungi; YBL033C_mRNA; YBL033C; YBL033C.
DR GeneID; 852247; -.
DR KEGG; sce:YBL033C; -.
DR SGD; S000000129; RIB1.
DR VEuPathDB; FungiDB:YBL033C; -.
DR eggNOG; KOG1284; Eukaryota.
DR GeneTree; ENSGT00940000176677; -.
DR HOGENOM; CLU_020273_2_4_1; -.
DR InParanoid; P38066; -.
DR OMA; RLPNVEC; -.
DR BioCyc; MetaCyc:YBL033C-MON; -.
DR BioCyc; YEAST:YBL033C-MON; -.
DR UniPathway; UPA00275; UER00400.
DR PRO; PR:P38066; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38066; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0019238; F:cyclohydrolase activity; IMP:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IMP:SGD.
DR CDD; cd00641; GTP_cyclohydro2; 1.
DR Gene3D; 3.40.50.10990; -; 1.
DR InterPro; IPR032677; GTP_cyclohydro_II.
DR InterPro; IPR000926; RibA.
DR InterPro; IPR036144; RibA-like_sf.
DR Pfam; PF00925; GTP_cyclohydro2; 1.
DR SUPFAM; SSF142695; SSF142695; 2.
DR TIGRFAMs; TIGR00505; ribA; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Riboflavin biosynthesis; Zinc.
FT CHAIN 1..345
FT /note="GTP cyclohydrolase-2"
FT /id="PRO_0000151786"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 233
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 143..147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 197..199
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 345 AA; 38332 MW; D98D561CEB21A7D1 CRC64;
MTIDNYDNSK QDSSKYEVSG TGDGRNGDGG LPLVQCVARA RIPTTQGPDI FLHLYSNNRD
NKEHLAIVFG EDIRSRSLFR RRQCETQQDR MIRGAYIGKL YPGRTVADED DRLGLALEFD
DSTGELLASK ATTWDAHNDT LVRIHSECYT GENAWSARCD CGEQFDRAGR LIACDHEPTS
NIKGGNGHGV IVYLRQEGRG IGLGEKLKAY NLQDLGADTV QANLMLKHPV DARDFSLGKA
ILLDLGIGNV RLLTNNPEKI KQVDHAPYLK CVERVPMVPI HWTNSSEGID SKEIEGYLRT
KIERMGHLLT EPLKLHTNPQ PTETSEAQNQ NRMNSALSST STLAI
