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Protein

GTP cyclohydrolase FolE2 2

Gene

folE2-2

Organism
Dechloromonas aromatica (strain RCB)
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei152 – 1521May be catalytically importantUniRule annotation

GO - Molecular functioni

  1. GTP cyclohydrolase I activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 7,8-dihydroneopterin 3'-triphosphate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciDARO159087:GI5B-3135-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 lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas
ProteomesiUP000000550 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 270270GTP cyclohydrolase FolE2 2PRO_0000289487Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi159087.Daro_3062.

Structurei

3D structure databases

ProteinModelPortaliQ47BI9.
SMRiQ47BI9. Positions 19-263.
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.

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.
RefSeqiYP_286262.1. NC_007298.1.

Genome annotation databases

EnsemblBacteriaiAAZ47792; AAZ47792; Daro_3062.
KEGGidar:Daro_3062.
PATRICi21604792. VBIDecAro89105_3041.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000089 Genomic DNA. Translation: AAZ47792.1.
RefSeqiYP_286262.1. NC_007298.1.

3D structure databases

ProteinModelPortaliQ47BI9.
SMRiQ47BI9. Positions 19-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi159087.Daro_3062.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ47792; AAZ47792; Daro_3062.
KEGGidar:Daro_3062.
PATRICi21604792. VBIDecAro89105_3041.

Phylogenomic databases

eggNOGiCOG1469.
HOGENOMiHOG000280679.
KOiK09007.
OMAiGAHNQRG.
OrthoDBiEOG6X6RBH.

Enzyme and pathway databases

UniPathwayiUPA00848; UER00151.
BioCyciDARO159087:GI5B-3135-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. "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
    Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
    BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RCB.

Entry informationi

Entry nameiGCH42_DECAR
AccessioniPrimary (citable) accession number: Q47BI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: September 13, 2005
Last modified: April 1, 2015
This is version 55 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.