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Protein

GTP cyclohydrolase-2

Gene

RIB1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.By similarity

Catalytic activityi

GTP + 3 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathwayi: riboflavin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-amino-6-(D-ribitylamino)uracil from GTP.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. GTP cyclohydrolase-2 (RIB1)
  2. Bifunctional protein RIB2 (RIB2)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
This subpathway is part of the pathway riboflavin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-6-(D-ribitylamino)uracil from GTP, the pathway riboflavin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi148 – 1481Zinc; catalyticBy similarity
Metal bindingi159 – 1591Zinc; catalyticBy similarity
Metal bindingi161 – 1611Zinc; catalyticBy similarity
Binding sitei164 – 1641GTPBy similarity
Binding sitei219 – 2191GTPBy similarity
Active sitei231 – 2311Proton acceptorSequence analysis
Active sitei233 – 2331NucleophileBy similarity
Binding sitei254 – 2541GTPBy similarity
Binding sitei259 – 2591GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi143 – 1475GTPBy similarity
Nucleotide bindingi197 – 1993GTPBy similarity

GO - Molecular functioni

  • cyclohydrolase activity Source: SGD
  • GTP binding Source: UniProtKB-KW
  • GTP cyclohydrolase II activity Source: UniProtKB-EC
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • riboflavin biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Riboflavin biosynthesis

Keywords - Ligandi

GTP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:YBL033C-MONOMER.
YEAST:YBL033C-MONOMER.
UniPathwayiUPA00275; UER00400.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase-2 (EC:3.5.4.25)
Alternative name(s):
GTP cyclohydrolase II
Gene namesi
Name:RIB1
Ordered Locus Names:YBL033C
ORF Names:YBL0417
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL033C.
SGDiS000000129. RIB1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345GTP cyclohydrolase-2PRO_0000151786Add
BLAST

Proteomic databases

MaxQBiP38066.
PeptideAtlasiP38066.

PTM databases

iPTMnetiP38066.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-7436,EBI-7436

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi32664. 8 interactions.
DIPiDIP-3936N.
IntActiP38066. 6 interactions.
MINTiMINT-497765.

Structurei

3D structure databases

ProteinModelPortaliP38066.
SMRiP38066. Positions 29-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GTP cyclohydrolase II family.Curated

Phylogenomic databases

HOGENOMiHOG000115443.
InParanoidiP38066.
KOiK01497.
OMAiEIFLHLY.
OrthoDBiEOG7SFJ5H.

Family and domain databases

InterProiIPR032677. GTP_cyclohydro_II.
IPR000926. RibA.
[Graphical view]
PfamiPF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
SUPFAMiSSF142695. SSF142695. 2 hits.
TIGRFAMsiTIGR00505. ribA. 1 hit.

Sequencei

Sequence statusi: Complete.

P38066-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIDNYDNSK QDSSKYEVSG TGDGRNGDGG LPLVQCVARA RIPTTQGPDI
60 70 80 90 100
FLHLYSNNRD NKEHLAIVFG EDIRSRSLFR RRQCETQQDR MIRGAYIGKL
110 120 130 140 150
YPGRTVADED DRLGLALEFD DSTGELLASK ATTWDAHNDT LVRIHSECYT
160 170 180 190 200
GENAWSARCD CGEQFDRAGR LIACDHEPTS NIKGGNGHGV IVYLRQEGRG
210 220 230 240 250
IGLGEKLKAY NLQDLGADTV QANLMLKHPV DARDFSLGKA ILLDLGIGNV
260 270 280 290 300
RLLTNNPEKI KQVDHAPYLK CVERVPMVPI HWTNSSEGID SKEIEGYLRT
310 320 330 340
KIERMGHLLT EPLKLHTNPQ PTETSEAQNQ NRMNSALSST STLAI
Length:345
Mass (Da):38,332
Last modified:December 15, 1998 - v2
Checksum:iD98D561CEB21A7D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35794 Genomic DNA. Translation: CAA84853.1.
X74738 Genomic DNA. Translation: CAA52759.1.
Z21617 Genomic DNA. Translation: CAA79741.1.
BK006936 Genomic DNA. Translation: DAA07086.1.
PIRiS45767.
RefSeqiNP_009520.1. NM_001178273.1.

Genome annotation databases

EnsemblFungiiYBL033C; YBL033C; YBL033C.
GeneIDi852247.
KEGGisce:YBL033C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35794 Genomic DNA. Translation: CAA84853.1.
X74738 Genomic DNA. Translation: CAA52759.1.
Z21617 Genomic DNA. Translation: CAA79741.1.
BK006936 Genomic DNA. Translation: DAA07086.1.
PIRiS45767.
RefSeqiNP_009520.1. NM_001178273.1.

3D structure databases

ProteinModelPortaliP38066.
SMRiP38066. Positions 29-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32664. 8 interactions.
DIPiDIP-3936N.
IntActiP38066. 6 interactions.
MINTiMINT-497765.

PTM databases

iPTMnetiP38066.

Proteomic databases

MaxQBiP38066.
PeptideAtlasiP38066.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL033C; YBL033C; YBL033C.
GeneIDi852247.
KEGGisce:YBL033C.

Organism-specific databases

EuPathDBiFungiDB:YBL033C.
SGDiS000000129. RIB1.

Phylogenomic databases

HOGENOMiHOG000115443.
InParanoidiP38066.
KOiK01497.
OMAiEIFLHLY.
OrthoDBiEOG7SFJ5H.

Enzyme and pathway databases

UniPathwayiUPA00275; UER00400.
BioCyciMetaCyc:YBL033C-MONOMER.
YEAST:YBL033C-MONOMER.

Miscellaneous databases

NextBioi970811.
PROiP38066.

Family and domain databases

InterProiIPR032677. GTP_cyclohydro_II.
IPR000926. RibA.
[Graphical view]
PfamiPF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
SUPFAMiSSF142695. SSF142695. 2 hits.
TIGRFAMsiTIGR00505. ribA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of an 8.8 kb segment on the left arm of chromosome II from Saccharomyces cerevisiae reveals four new open reading frames including homologs of animal DNA polymerase alpha-primases and bacterial GTP cyclohydrolase II."
    Skala J., van Dyck L., Purnelle B., Goffeau A.
    Yeast 10:S13-S24(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Skala J., van Dyck L., Purnelle B., Goffeau A.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 181.
  3. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRIB1_YEAST
AccessioniPrimary (citable) accession number: P38066
Secondary accession number(s): D6VPW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: December 15, 1998
Last modified: May 11, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 9520 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.