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Q9X8I3 (GCH1_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 95. 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:SCO3403
ORF Names:SCE9.10c
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group

Protein attributes

Sequence length201 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 – 201201GTP cyclohydrolase 1 HAMAP-Rule MF_00223
PRO_0000119447

Sites

Metal binding901Zinc By similarity
Metal binding931Zinc By similarity
Metal binding1631Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9X8I3 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 4CC8FE6E76687B6B

FASTA20122,415
        10         20         30         40         50         60 
MTDPVTLDGE GQIGEFDEKR AENAVRELLI AVGEDPDREG LRETPARVAR AYREIFAGLW 

        70         80         90        100        110        120 
QEPEDVLTTT FDLGHDEMVL VKDIEVFSTC EHHLVPFRGV AHVGYIPSTS GKITGLSKLA 

       130        140        150        160        170        180 
RLVDVYARRP QVQERLTTQI ADSLMEILEP RGVIVVVECE HMCMSMRGIR KPGAKTLTSA 

       190        200 
VRGQLRDVAT RNEAMSLIMA R 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939116 Genomic DNA. Translation: CAB42756.1.
PIRT36329.
RefSeqNP_627609.1. NC_003888.3.

3D structure databases

ProteinModelPortalQ9X8I3.
SMRQ9X8I3. Positions 15-198.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO3403.

PTM databases

PhosSiteP12011338.

Proteomic databases

PRIDEQ9X8I3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB42756; CAB42756; CAB42756.
GeneID1098840.
KEGGsco:SCO3403.
PATRIC23736562. VBIStrCoe124346_3466.

Phylogenomic databases

eggNOGCOG0302.
HOGENOMHOG000221222.
KOK01495.
OMAVYSHCEH.
OrthoDBEOG6XHC8G.
PhylomeDBQ9X8I3.

Enzyme and pathway databases

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_STRCO
AccessionPrimary (citable) accession number: Q9X8I3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: May 14, 2014
This is version 95 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