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Q82VD1 (GCH4_NITEU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP cyclohydrolase FolE2

EC=3.5.4.16
Gene names
Name:folE2
Ordered Locus Names:NE1163
OrganismNitrosomonas europaea (strain ATCC 19718 / NBRC 14298) [Complete proteome] [HAMAP]
Taxonomic identifier228410 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

Protein attributes

Sequence length268 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts GTP to 7,8-dihydroneopterin triphosphate By similarity. HAMAP-Rule MF_01527

Catalytic activity

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. HAMAP-Rule MF_01527

Pathway

Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP-Rule MF_01527

Sequence similarities

Belongs to the GTP cyclohydrolase IV family.

Ontologies

Keywords
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_process7,8-dihydroneopterin 3'-triphosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionGTP cyclohydrolase I activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 268268GTP cyclohydrolase FolE2 HAMAP-Rule MF_01527
PRO_0000147717

Sites

Site1541May be catalytically important By similarity

Secondary structure

....................................... 268
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q82VD1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: DAA9B16495ED23E4

FASTA26830,604
        10         20         30         40         50         60 
MNKQIDLPIA DVQGSLDTRH IAIDRVGIKA IRHPVVVADK GGGSQHTVAQ FNMYVNLPHN 

        70         80         90        100        110        120 
FKGTHMSRFV EILNSHEREI SVESFEEILR SMVSRLESDS GHIEMAFPYF INKSAPVSGV 

       130        140        150        160        170        180 
KSLLDYEVTF IGEIKHGNQY SFTMKVIVPV TSLCPCSKKI SDYGAHNQRS HVTISVRTNS 

       190        200        210        220        230        240 
FIWIEDIIRI AEEQASCELY GLLKRPDEKY VTERAYNNPK FVEDIVRDVA EVLNHDDRID 

       250        260 
AYIVESENFE SIHNHSAYAL IERDKRIR 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea."
Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.
J. Bacteriol. 185:2759-2773(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19718 / NBRC 14298.
[2]"The crystal structure of duf198 from Nitrosomonas europaea ATCC 19718."
Midwest center for structural genomics (MCSG)
Submitted (SEP-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL954747 Genomic DNA. Translation: CAD85074.1.
RefSeqNP_841220.1. NC_004757.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2R5RX-ray3.05A1-268[»]
ProteinModelPortalQ82VD1.
SMRQ82VD1. Positions 20-265.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING228410.NE1163.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD85074; CAD85074; NE1163.
GeneID1082107.
KEGGneu:NE1163.
PATRIC22713382. VBINitEur56163_1290.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1469.
HOGENOMHOG000280679.
KOK09007.
OMADVQSSRD.
OrthoDBEOG6X6RBH.
PhylomeDBQ82VD1.

Enzyme and pathway databases

BioCycNEUR228410:GJNO-1188-MONOMER.
UniPathwayUPA00848; UER00151.

Family and domain databases

HAMAPMF_01527_B. GTP_cyclohydrol_B.
InterProIPR022838. GTP_cyclohydrolase_FolE2.
IPR003801. GTP_cyclohydrolase_FolE2/MptA.
[Graphical view]
PfamPF02649. GCHY-1. 1 hit.
[Graphical view]
TIGRFAMsTIGR00294. TIGR00294. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ82VD1.

Entry information

Entry nameGCH4_NITEU
AccessionPrimary (citable) accession number: Q82VD1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways