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Q5HWX4 (GCH1_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:CJE0187
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length190 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 – 190190GTP cyclohydrolase 1 HAMAP-Rule MF_00223
PRO_1000043674

Sites

Metal binding751Zinc By similarity
Metal binding781Zinc By similarity
Metal binding1461Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HWX4 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 57728A231F2BFB4C

FASTA19021,752
        10         20         30         40         50         60 
MQKKFEDCVK TILEIIGENP NREGLIKTPN RVFKAYEFLA SGYTQNVKDI LNDALFESSN 

        70         80         90        100        110        120 
NEMVLVRDIE FYSLCEHHLL PFFGRAHVAY IPNKKVVGLS KIPRLVEVFA RRLQIQEQLT 

       130        140        150        160        170        180 
EQIAQALMEN VDAKGVGVVI EARHMCVEMR GIQKANSTTT TSALRGIFLK NEKTREEFFS 

       190 
LINSAKQVRF 

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM1221.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000025 Genomic DNA. Translation: AAW34782.1.
RefSeqYP_178211.1. NC_003912.7.

3D structure databases

ProteinModelPortalQ5HWX4.
SMRQ5HWX4. Positions 3-184.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195099.CJE0187.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW34782; AAW34782; CJE0187.
GeneID3230950.
KEGGcjr:CJE0187.
PATRIC20042083. VBICamJej134361_0191.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0302.
HOGENOMHOG000221222.
KOK01495.
OMAGENPARE.
OrthoDBEOG6XHC8G.

Enzyme and pathway databases

BioCycCJEJ195099:GJC0-192-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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGCH1_CAMJR
AccessionPrimary (citable) accession number: Q5HWX4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 62 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