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Reviewed, UniProtKB/Swiss-Prot Q5HWX4 (GCH1_CAMJR)

Last modified November 3, 2009. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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.
Sequence processingThe displayed sequence is not processed.
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 MF_00223

Pathway

Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP 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 MF_00223
PRO_1000043674

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q5HWX4-1 [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: 15660156] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000025 Genomic DNA. Translation: AAW34782.1.
RefSeqYP_178211.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HWX4.

Genome annotation databases

GeneID3230950.
GenomeReviewsGene locus CJE0187 in contig CP000025_GR.
KEGGcjr:CJE0187.
NMPDRfig|195099.3.peg.45.
TIGRCJE0187.

Phylogenomic databases

HOGENOMQ5HWX4.
OMAARIVEMF.

Enzyme and pathway databases

BioCycCJEJ195099:CJE_0187-MON.

Family and domain databases

HAMAPMF_00223.
[Tree]
InterProIPR001474. GTP_CycHdrlase_I.
IPR020602. GTP_CycHdrlase_I/CN_OxRdtase.
IPR018234. GTP_CycHdrlase_I_CS.
[Graphical view]
PANTHERPTHR11109. GTP_cyclohydro_I. 1 hit.
PfamPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
ProDomPD003330. GTP_cyclohydroI. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00063. folE. 1 hit.
PROSITEPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. False negative.
[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: November 3, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents