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P64208 (GCH1_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 63. 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
Synonyms:gchA
Ordered Locus Names:Mb3639c
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length202 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 – 202202GTP cyclohydrolase 1 HAMAP-Rule MF_00223
PRO_0000119424

Sites

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

Sequences

Sequence LengthMass (Da)Tools
P64208 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 7ED8293B83CB39DC

FASTA20222,395
        10         20         30         40         50         60 
MSQLDSRSAS ARIRVFDQQR AEAAVRELLY AIGEDPDRDG LVATPSRVAR SYREMFAGLY 

        70         80         90        100        110        120 
TDPDSVLNTM FDEDHDELVL VKEIPMYSTC EHHLVAFHGV AHVGYIPGDD GRVTGLSKIA 

       130        140        150        160        170        180 
RLVDLYAKRP QVQERLTSQI ADALMKKLDP RGVIVVIEAE HLCMAMRGVR KPGSVTTTSA 

       190        200 
VRGLFKTNAA SRAEALDLIL RK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248333 Genomic DNA. Translation: CDO44910.1.
RefSeqNP_857278.1. NC_002945.3.

3D structure databases

ProteinModelPortalP64208.
SMRP64208. Positions 23-199.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233413.Mb3639c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD95825; CAD95825; Mb3639c.
GeneID1093567.
KEGGmbo:Mb3639c.
PATRIC18009715. VBIMycBov88188_3985.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0302.
HOGENOMHOG000221222.
KOK01495.
OMAYEQIEYA.
OrthoDBEOG6XHC8G.

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_MYCBO
AccessionPrimary (citable) accession number: P64208
Secondary accession number(s): O06273, X2BPE3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: June 11, 2014
This is version 63 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