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Q0I3F6

- GCH1_HISS1

UniProt

Q0I3F6 - GCH1_HISS1

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Protein

GTP cyclohydrolase 1

Gene

folE

Organism
Histophilus somni (strain 129Pt) (Haemophilus somnus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi109 – 1091ZincUniRule annotation
Metal bindingi112 – 1121ZincUniRule annotation
Metal bindingi180 – 1801ZincUniRule annotation

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. GTP cyclohydrolase I activity Source: UniProtKB-HAMAP
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 7,8-dihydroneopterin 3'-triphosphate biosynthetic process Source: UniProtKB-UniPathway
  2. one-carbon metabolic process Source: UniProtKB-HAMAP
  3. tetrahydrofolate biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

GTP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciHSOM205914:GJ7V-943-MONOMER.
UniPathwayiUPA00848; UER00151.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase 1UniRule annotation (EC:3.5.4.16UniRule annotation)
Alternative name(s):
GTP cyclohydrolase IUniRule annotation
Short name:
GTP-CH-IUniRule annotation
Gene namesi
Name:folEUniRule annotation
Ordered Locus Names:HS_0910
OrganismiHistophilus somni (strain 129Pt) (Haemophilus somnus)
Taxonomic identifieri205914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
ProteomesiUP000001970: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218GTP cyclohydrolase 1PRO_1000043697Add
BLAST

Proteomic databases

PRIDEiQ0I3F6.

Interactioni

Subunit structurei

Toroid-shaped homodecamer, composed of two pentamers of five dimers.By similarity

Protein-protein interaction databases

STRINGi205914.HS_0910.

Structurei

3D structure databases

ProteinModelPortaliQ0I3F6.
SMRiQ0I3F6. Positions 3-217.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GTP cyclohydrolase I family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0302.
HOGENOMiHOG000221222.
KOiK01495.
OrthoDBiEOG6XHC8G.

Family and domain databases

HAMAPiMF_00223. FolE.
InterProiIPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view]
PANTHERiPTHR11109. PTHR11109. 1 hit.
PfamiPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00063. folE. 1 hit.
PROSITEiPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0I3F6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNLSPEAIK VRNALVEKGI ETPMIDLVQD KDQRRQGIEQ HMREVIKLIG
60 70 80 90 100
LDLSDDSLEE TPARLSKMFI DEIFSGLDYA NFPKITNIEN RMKVSEMVLV
110 120 130 140 150
DDVTLTSTCE HHFVTIDGKV SVAYYPQKWV IGLSKINRVV AFFAQRPQVQ
160 170 180 190 200
ERLTQQILLA FQTILETEDV AVYVKATHFC VKCRGIKDTN SYTVTSAFGG
210
VFLDDRETRK EFLTLLKK
Length:218
Mass (Da):24,906
Last modified:October 3, 2006 - v1
Checksum:iBA50C72E315125F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000436 Genomic DNA. Translation: ABI25185.1.
RefSeqiYP_719120.1. NC_008309.1.

Genome annotation databases

EnsemblBacteriaiABI25185; ABI25185; HS_0910.
GeneIDi4240402.
KEGGihso:HS_0910.
PATRICi20281833. VBIHaeSom53361_0953.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000436 Genomic DNA. Translation: ABI25185.1 .
RefSeqi YP_719120.1. NC_008309.1.

3D structure databases

ProteinModelPortali Q0I3F6.
SMRi Q0I3F6. Positions 3-217.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 205914.HS_0910.

Proteomic databases

PRIDEi Q0I3F6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABI25185 ; ABI25185 ; HS_0910 .
GeneIDi 4240402.
KEGGi hso:HS_0910.
PATRICi 20281833. VBIHaeSom53361_0953.

Phylogenomic databases

eggNOGi COG0302.
HOGENOMi HOG000221222.
KOi K01495.
OrthoDBi EOG6XHC8G.

Enzyme and pathway databases

UniPathwayi UPA00848 ; UER00151 .
BioCyci HSOM205914:GJ7V-943-MONOMER.

Family and domain databases

HAMAPi MF_00223. FolE.
InterProi IPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view ]
PANTHERi PTHR11109. PTHR11109. 1 hit.
Pfami PF01227. GTP_cyclohydroI. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00063. folE. 1 hit.
PROSITEi PS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
    Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
    J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 129Pt.

Entry informationi

Entry nameiGCH1_HISS1
AccessioniPrimary (citable) accession number: Q0I3F6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: November 26, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3