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Q3SKF2

- GCH4_THIDA

UniProt

Q3SKF2 - GCH4_THIDA

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Protein
GTP cyclohydrolase FolE2
Gene
folE2, Tbd_0878
Organism
Thiobacillus denitrificans (strain ATCC 25259)
Status
Reviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

Converts GTP to 7,8-dihydroneopterin triphosphate By similarity.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
Sitei155 – 1551May be catalytically important By similarity

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

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

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase FolE2 (EC:3.5.4.16)
Gene namesi
Name:folE2
Ordered Locus Names:Tbd_0878
OrganismiThiobacillus denitrificans (strain ATCC 25259)
Taxonomic identifieri292415 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus
ProteomesiUP000008291: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 269269GTP cyclohydrolase FolE2UniRule annotation
PRO_0000289529Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi292415.Tbd_0878.

Structurei

3D structure databases

ProteinModelPortaliQ3SKF2.
SMRiQ3SKF2. Positions 22-266.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1469.
HOGENOMiHOG000280679.
KOiK09007.
OMAiDVQSSRD.
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

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MNEICDTAVC MPDVQSSADT RQIAIDKVGI KSIRHPVRVA DKADGVQHTI    50
ANFNMYVFLP HNFKGTHMSR FIEILNTRER EISVENFEGM LRQMVERLEA 100
ESGYIEMTFP YFINKSAPVS GVQSMLDYEV TFVGAIENGQ YTHTTKVVVP 150
VTSLCPCSKK ISEYGAHNQR SHVTVTAKTR GFLWIEDLVR KVEDQASCEL 200
FGLLKRPDEK YVTERAYDNP KFVEDIVRDV AAAMNAEPLI DAYVVEAENF 250
ESIHNHSAYA LIEHDKRKK 269
Length:269
Mass (Da):30,583
Last modified:October 11, 2005 - v1
Checksum:iF098030F47337DCC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000116 Genomic DNA. Translation: AAZ96831.1.
RefSeqiYP_314636.1. NC_007404.1.

Genome annotation databases

EnsemblBacteriaiAAZ96831; AAZ96831; Tbd_0878.
GeneIDi3671643.
KEGGitbd:Tbd_0878.
PATRICi23967921. VBIThiDen82923_0874.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000116 Genomic DNA. Translation: AAZ96831.1 .
RefSeqi YP_314636.1. NC_007404.1.

3D structure databases

ProteinModelPortali Q3SKF2.
SMRi Q3SKF2. Positions 22-266.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 292415.Tbd_0878.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAZ96831 ; AAZ96831 ; Tbd_0878 .
GeneIDi 3671643.
KEGGi tbd:Tbd_0878.
PATRICi 23967921. VBIThiDen82923_0874.

Phylogenomic databases

eggNOGi COG1469.
HOGENOMi HOG000280679.
KOi K09007.
OMAi DVQSSRD.
OrthoDBi EOG6X6RBH.

Enzyme and pathway databases

UniPathwayi UPA00848 ; UER00151 .
BioCyci TDEN292415:GHWG-900-MONOMER.

Family and domain databases

HAMAPi MF_01527_B. GTP_cyclohydrol_B.
InterProi IPR022838. GTP_cyclohydrolase_FolE2.
IPR003801. GTP_cyclohydrolase_FolE2/MptA.
[Graphical view ]
Pfami PF02649. GCHY-1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: May 14, 2014
This is version 54 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

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