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Protein

GTP cyclohydrolase FolE2 2

Gene

folE2-2

Organism
Dechloromonas aromatica (strain RCB)
Status
Reviewed-Annotation score: -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

Pathwayi: 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 FolE2 2 (folE2-2), GTP cyclohydrolase FolE2 1 (folE2-1)
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)DescriptionActionsGraphical viewLength
Sitei152May be catalytically importantUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase

Enzyme and pathway databases

BioCyciDARO159087:G1G4R-3161-MONOMER
UniPathwayiUPA00848; UER00151

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase FolE2 2UniRule annotation (EC:3.5.4.16UniRule annotation)
Gene namesi
Name:folE2-2UniRule annotation
Ordered Locus Names:Daro_3062
OrganismiDechloromonas aromatica (strain RCB)
Taxonomic identifieri159087 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesAzonexaceaeDechloromonas
Proteomesi
  • UP000000550 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002894871 – 270GTP cyclohydrolase FolE2 2Add BLAST270

Interactioni

Protein-protein interaction databases

STRINGi159087.Daro_3062

Structurei

3D structure databases

ProteinModelPortaliQ47BI9
SMRiQ47BI9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GTP cyclohydrolase IV family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DZA Bacteria
COG1469 LUCA
HOGENOMiHOG000280679
KOiK09007
OMAiHNQRGRG
OrthoDBiPOG091H0MIO

Family and domain databases

HAMAPiMF_01527_B GTP_cyclohydrol_B, 1 hit
InterProiView protein in InterPro
IPR022838 GTP_cyclohydrolase_FolE2
IPR003801 GTP_cyclohydrolase_FolE2/MptA
PANTHERiPTHR36445 PTHR36445, 1 hit
PfamiView protein in Pfam
PF02649 GCHY-1, 1 hit

Sequencei

Sequence statusi: Complete.

Q47BI9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTPTSNIPD VQNSADTRHI AINKVGIKSI RHPIKVQDKS AGIQHTIAMF
60 70 80 90 100
NMYVGLPHNF KGTHMSRFVE ILNSHEREIS VENFPTMLRD MVVKLEAETG
110 120 130 140 150
HIEMNFPYFI NKTAPVSGVQ SLMDYDVTFI GDICHGEIAT SVKVVVPVTS
160 170 180 190 200
LCPCSKKISE YGAHNQRSHV TVTAKTNDFM WIEEIVQLVE QEASCELFGL
210 220 230 240 250
LKRPDEKYVT ERAYDNPKFV EDMVRDVAAR LNAEARVDAY VVESENFESI
260 270
HNHSAYALIE NDKKNPLAHA
Length:270
Mass (Da):30,433
Last modified:September 13, 2005 - v1
Checksum:i9082AECA73AF9B78
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000089 Genomic DNA Translation: AAZ47792.1
RefSeqiWP_011288790.1, NC_007298.1

Genome annotation databases

EnsemblBacteriaiAAZ47792; AAZ47792; Daro_3062
KEGGidar:Daro_3062

Similar proteinsi

Entry informationi

Entry nameiGCH42_DECAR
AccessioniPrimary (citable) accession number: Q47BI9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: September 13, 2005
Last modified: March 28, 2018
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health