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Q8P3B0 (GCH1_XANCP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. 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:XCC4166
OrganismXanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP]
Taxonomic identifier190485 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length200 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 caution

The sequence AAM43382.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 200200GTP cyclohydrolase 1 HAMAP-Rule MF_00223
PRO_0000119467

Sites

Metal binding871Zinc By similarity
Metal binding901Zinc By similarity
Metal binding1581Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8P3B0 [UniParc].

Last modified November 15, 2002. Version 2.
Checksum: 732CB3CE0AF4F912

FASTA20022,556
        10         20         30         40         50         60 
MSQSDQPDSS VTQAQAEEAV RTLLRWAGED PAREGLLDTP RRVAEAYGDW FSGYREEPRA 

        70         80         90        100        110        120 
YLERTFEEVA GYDELIVLRD ISYESHCEHH MAPIIGKVHV GYLPRGKVVG ISKLARVVES 

       130        140        150        160        170        180 
YARRFQVQEK MTAQIAQCIQ DVLQPRGVGV VVEGAHECMT TRGIHKRGVS MVTSKMLGSF 

       190        200 
REDARTRAEF LQFIEVGGKR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008922 Genomic DNA. Translation: AAM43382.1. Different initiation.
RefSeqNP_639500.1. NC_003902.1.

3D structure databases

ProteinModelPortalQ8P3B0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190485.XCC4166.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM43382; AAM43382; XCC4166.
GeneID1001199.
KEGGxcc:XCC4166.
PATRIC24079584. VBIXanCam115730_4463.

Phylogenomic databases

eggNOGCOG0302.
HOGENOMHOG000221222.
KOK01495.
OMASWKEERT.
OrthoDBEOG6XHC8G.

Enzyme and pathway databases

BioCycXCAM190485:GIXZ-4164-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_XANCP
AccessionPrimary (citable) accession number: Q8P3B0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 15, 2002
Last modified: May 14, 2014
This is version 80 of the entry and version 2 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