Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

GTP cyclohydrolase FolE2

Gene

folE2

Organism
Thiobacillus denitrificans (strain ATCC 25259)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Converts GTP to 7,8-dihydroneopterin triphosphate.UniRule annotation

Catalytic activityi

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

Pathway: 7,8-dihydroneopterin triphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 7,8-dihydroneopterin triphosphate from GTP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. GTP cyclohydrolase 1 (folE), GTP cyclohydrolase 1 (Tbd_0481), GTP cyclohydrolase FolE2 (folE2)
This subpathway is part of the pathway 7,8-dihydroneopterin triphosphate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 7,8-dihydroneopterin triphosphate from GTP, the pathway 7,8-dihydroneopterin triphosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei155 – 1551May be catalytically importantUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciTDEN292415:GHWG-900-MONOMER.
UniPathwayiUPA00848; UER00151.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase FolE2UniRule annotation (EC:3.5.4.16UniRule annotation)
Gene namesi
Name:folE2UniRule annotation
Ordered Locus Names:Tbd_0878
OrganismiThiobacillus denitrificans (strain ATCC 25259)
Taxonomic identifieri292415 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus
ProteomesiUP000008291 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 269269GTP cyclohydrolase FolE2PRO_0000289529Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi292415.Tbd_0878.

Structurei

3D structure databases

ProteinModelPortaliQ3SKF2.
SMRiQ3SKF2. Positions 22-266.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GTP cyclohydrolase IV family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1469.
HOGENOMiHOG000280679.
KOiK09007.
OMAiGAHNQRG.
OrthoDBiEOG6X6RBH.

Family and domain databases

HAMAPiMF_01527_B. GTP_cyclohydrol_B.
InterProiIPR022838. GTP_cyclohydrolase_FolE2.
IPR003801. GTP_cyclohydrolase_FolE2/MptA.
[Graphical view]
PfamiPF02649. GCHY-1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3SKF2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEICDTAVC MPDVQSSADT RQIAIDKVGI KSIRHPVRVA DKADGVQHTI
60 70 80 90 100
ANFNMYVFLP HNFKGTHMSR FIEILNTRER EISVENFEGM LRQMVERLEA
110 120 130 140 150
ESGYIEMTFP YFINKSAPVS GVQSMLDYEV TFVGAIENGQ YTHTTKVVVP
160 170 180 190 200
VTSLCPCSKK ISEYGAHNQR SHVTVTAKTR GFLWIEDLVR KVEDQASCEL
210 220 230 240 250
FGLLKRPDEK YVTERAYDNP KFVEDIVRDV AAAMNAEPLI DAYVVEAENF
260
ESIHNHSAYA LIEHDKRKK
Length:269
Mass (Da):30,583
Last modified:October 11, 2005 - v1
Checksum:iF098030F47337DCC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000116 Genomic DNA. Translation: AAZ96831.1.
RefSeqiWP_011311390.1. NC_007404.1.
YP_314636.1. NC_007404.1.

Genome annotation databases

EnsemblBacteriaiAAZ96831; AAZ96831; Tbd_0878.
KEGGitbd:Tbd_0878.
PATRICi23967921. VBIThiDen82923_0874.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000116 Genomic DNA. Translation: AAZ96831.1.
RefSeqiWP_011311390.1. NC_007404.1.
YP_314636.1. NC_007404.1.

3D structure databases

ProteinModelPortaliQ3SKF2.
SMRiQ3SKF2. Positions 22-266.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi292415.Tbd_0878.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ96831; AAZ96831; Tbd_0878.
KEGGitbd:Tbd_0878.
PATRICi23967921. VBIThiDen82923_0874.

Phylogenomic databases

eggNOGiCOG1469.
HOGENOMiHOG000280679.
KOiK09007.
OMAiGAHNQRG.
OrthoDBiEOG6X6RBH.

Enzyme and pathway databases

UniPathwayiUPA00848; UER00151.
BioCyciTDEN292415:GHWG-900-MONOMER.

Family and domain databases

HAMAPiMF_01527_B. GTP_cyclohydrol_B.
InterProiIPR022838. GTP_cyclohydrolase_FolE2.
IPR003801. GTP_cyclohydrolase_FolE2/MptA.
[Graphical view]
PfamiPF02649. GCHY-1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans."
    Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.
    J. Bacteriol. 188:1473-1488(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25259.

Entry informationi

Entry nameiGCH4_THIDA
AccessioniPrimary (citable) accession number: Q3SKF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 11, 2005
Last modified: April 29, 2015
This is version 60 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, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.