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P38066 (RIB1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP cyclohydrolase-2

EC=3.5.4.25
Alternative name(s):
GTP cyclohydrolase II
Gene names
Name:RIB1
Ordered Locus Names:YBL033C
ORF Names:YBL0417
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.

Miscellaneous

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

Sequence similarities

Belongs to the GTP cyclohydrolase II family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-7436,EBI-7436

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345GTP cyclohydrolase-2
PRO_0000151786

Regions

Nucleotide binding143 – 1475GTP By similarity
Nucleotide binding197 – 1993GTP By similarity

Sites

Active site2311Proton acceptor Potential
Active site2331Nucleophile By similarity
Metal binding1481Zinc; catalytic By similarity
Metal binding1591Zinc; catalytic By similarity
Metal binding1611Zinc; catalytic By similarity
Binding site1641GTP By similarity
Binding site2191GTP By similarity
Binding site2541GTP By similarity
Binding site2591GTP By similarity

Amino acid modifications

Modified residue2851Phosphoserine Ref.6

Sequences

Sequence LengthMass (Da)Tools
P38066 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: D98D561CEB21A7D1

FASTA34538,332
        10         20         30         40         50         60 
MTIDNYDNSK QDSSKYEVSG TGDGRNGDGG LPLVQCVARA RIPTTQGPDI FLHLYSNNRD 

        70         80         90        100        110        120 
NKEHLAIVFG EDIRSRSLFR RRQCETQQDR MIRGAYIGKL YPGRTVADED DRLGLALEFD 

       130        140        150        160        170        180 
DSTGELLASK ATTWDAHNDT LVRIHSECYT GENAWSARCD CGEQFDRAGR LIACDHEPTS 

       190        200        210        220        230        240 
NIKGGNGHGV IVYLRQEGRG IGLGEKLKAY NLQDLGADTV QANLMLKHPV DARDFSLGKA 

       250        260        270        280        290        300 
ILLDLGIGNV RLLTNNPEKI KQVDHAPYLK CVERVPMVPI HWTNSSEGID SKEIEGYLRT 

       310        320        330        340 
KIERMGHLLT EPLKLHTNPQ PTETSEAQNQ NRMNSALSST STLAI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z35794 Genomic DNA. Translation: CAA84853.1.
X74738 Genomic DNA. Translation: CAA52759.1.
Z21617 Genomic DNA. Translation: CAA79741.1.
BK006936 Genomic DNA. Translation: DAA07086.1.
PIRS45767.
RefSeqNP_009520.1. NM_001178273.1.

3D structure databases

ProteinModelPortalP38066.
SMRP38066. Positions 136-278.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-3936N.
IntActP38066. 6 interactions.
MINTMINT-497765.
STRING4932.YBL033C.

Proteomic databases

PaxDbP38066.
PeptideAtlasP38066.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBL033C; YBL033C; YBL033C.
GeneID852247.
KEGGsce:YBL033C.

Organism-specific databases

CYGDYBL033c.
SGDS000000129. RIB1.

Phylogenomic databases

eggNOGCOG0807.
HOGENOMHOG000115443.
KOK01497.
OMARSYGLAT.
OrthoDBEOG4RBTTG.

Enzyme and pathway databases

BioCycMetaCyc:YBL033C-MONOMER.
UniPathwayUPA00275; UER00400.

Gene expression databases

GenevestigatorP38066.
GermOnlineYBL033C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000926. GTP_CycHdrlaseII_RibA.
[Graphical view]
PfamPF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00505. ribA. 1 hit.
ProtoNetSearch...

Other

NextBio970811.

Entry information

Entry nameRIB1_YEAST
AccessionPrimary (citable) accession number: P38066
Secondary accession number(s): D6VPW6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: December 15, 1998
Last modified: May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families