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Q5M391 (GCH1_STRT2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP cyclohydrolase 1

EC=3.5.4.16
Alternative name(s):
GTP cyclohydrolase I
Short name=GTP-CH-I
Gene names
Name:folE
Ordered Locus Names:stu1544
OrganismStreptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) [Complete proteome] [HAMAP]
Taxonomic identifier264199 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length187 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. HAMAP-Rule MF_00223

Pathway

Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP-Rule MF_00223

Subunit structure

Toroid-shaped homodecamer, composed of two pentamers of five dimers By similarity.

Sequence similarities

Belongs to the GTP cyclohydrolase I family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 187187GTP cyclohydrolase 1 HAMAP-Rule MF_00223
PRO_1000043751

Sites

Metal binding761Zinc By similarity
Metal binding791Zinc By similarity
Metal binding1481Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5M391 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 3AF6412D81A44A5A

FASTA18721,220
        10         20         30         40         50         60 
MENQEKVEQA VYQLLEALGE NPEREGLLDT PKRVAKMYAE MFSGLNEDPK DQFTAVFSEV 

        70         80         90        100        110        120 
HDEVVLVKDI PFYSMCEHHL VPFYGMAHVA YLPSGDKVTG LSKLARAVEV AARRPQLQER 

       130        140        150        160        170        180 
LTDQVATALE EALNPRGVFV MVEAEHMCMT MRGIKKPGSK TITTVAKGIY KEDREERKEI 


LSLMRDF 

« Hide

References

[1]"Complete sequence and comparative genome analysis of the dairy bacterium Streptococcus thermophilus."
Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D., Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D., Hancy F. expand/collapse author list , Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.
Nat. Biotechnol. 22:1554-1558(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-250 / LMG 18311.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000023 Genomic DNA. Translation: AAV61147.1.
RefSeqYP_139962.1. NC_006448.1.

3D structure databases

ProteinModelPortalQ5M391.
SMRQ5M391. Positions 3-186.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264199.stu1544.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV61147; AAV61147; stu1544.
GeneID3165556.
KEGGstl:stu1544.
PATRIC19804632. VBIStrThe97850_1514.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0302.
HOGENOMHOG000221222.
KOK01495.
OMAYEQIEYA.
OrthoDBEOG6XHC8G.

Enzyme and pathway databases

BioCycSTHE264199:GI6K-1490-MONOMER.
UniPathwayUPA00848; UER00151.

Family and domain databases

HAMAPMF_00223. FolE.
InterProIPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view]
PANTHERPTHR11109. PTHR11109. 1 hit.
PfamPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
TIGRFAMsTIGR00063. folE. 1 hit.
PROSITEPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGCH1_STRT2
AccessionPrimary (citable) accession number: Q5M391
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 1, 2005
Last modified: May 14, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways