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Q82VD1

- GCH4_NITEU

UniProt

Q82VD1 - GCH4_NITEU

Protein

GTP cyclohydrolase FolE2

Gene

folE2

Organism
Nitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    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
    Sitei154 – 1541May 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

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciNEUR228410:GJNO-1188-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:NE1163
    OrganismiNitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
    Taxonomic identifieri228410 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
    ProteomesiUP000001416: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 268268GTP cyclohydrolase FolE2PRO_0000147717Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi228410.NE1163.

    Structurei

    Secondary structure

    1
    268
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 3714
    Turni40 – 423
    Beta strandi45 – 5713
    Helixi63 – 675
    Helixi68 – 758
    Beta strandi78 – 814
    Helixi82 – 843
    Helixi85 – 9511
    Beta strandi99 – 11416
    Turni116 – 1183
    Beta strandi121 – 13515
    Turni136 – 1383
    Beta strandi139 – 15315
    Helixi155 – 1606
    Beta strandi161 – 1633
    Beta strandi167 – 18014
    Helixi184 – 19411
    Beta strandi195 – 1984
    Helixi205 – 21612
    Helixi222 – 23413
    Beta strandi239 – 24911
    Turni251 – 2533
    Beta strandi254 – 26411

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2R5RX-ray3.05A1-268[»]
    ProteinModelPortaliQ82VD1.
    SMRiQ82VD1. Positions 20-265.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ82VD1.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GTP cyclohydrolase IV family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1469.
    HOGENOMiHOG000280679.
    KOiK09007.
    OMAiDVQSSRD.
    OrthoDBiEOG6X6RBH.
    PhylomeDBiQ82VD1.

    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]
    TIGRFAMsiTIGR00294. TIGR00294. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q82VD1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKQIDLPIA DVQGSLDTRH IAIDRVGIKA IRHPVVVADK GGGSQHTVAQ    50
    FNMYVNLPHN FKGTHMSRFV EILNSHEREI SVESFEEILR SMVSRLESDS 100
    GHIEMAFPYF INKSAPVSGV KSLLDYEVTF IGEIKHGNQY SFTMKVIVPV 150
    TSLCPCSKKI SDYGAHNQRS HVTISVRTNS FIWIEDIIRI AEEQASCELY 200
    GLLKRPDEKY VTERAYNNPK FVEDIVRDVA EVLNHDDRID AYIVESENFE 250
    SIHNHSAYAL IERDKRIR 268
    Length:268
    Mass (Da):30,604
    Last modified:June 1, 2003 - v1
    Checksum:iDAA9B16495ED23E4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL954747 Genomic DNA. Translation: CAD85074.1.
    RefSeqiNP_841220.1. NC_004757.1.

    Genome annotation databases

    EnsemblBacteriaiCAD85074; CAD85074; NE1163.
    GeneIDi1082107.
    KEGGineu:NE1163.
    PATRICi22713382. VBINitEur56163_1290.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL954747 Genomic DNA. Translation: CAD85074.1 .
    RefSeqi NP_841220.1. NC_004757.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2R5R X-ray 3.05 A 1-268 [» ]
    ProteinModelPortali Q82VD1.
    SMRi Q82VD1. Positions 20-265.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 228410.NE1163.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAD85074 ; CAD85074 ; NE1163 .
    GeneIDi 1082107.
    KEGGi neu:NE1163.
    PATRICi 22713382. VBINitEur56163_1290.

    Phylogenomic databases

    eggNOGi COG1469.
    HOGENOMi HOG000280679.
    KOi K09007.
    OMAi DVQSSRD.
    OrthoDBi EOG6X6RBH.
    PhylomeDBi Q82VD1.

    Enzyme and pathway databases

    UniPathwayi UPA00848 ; UER00151 .
    BioCyci NEUR228410:GJNO-1188-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q82VD1.

    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 ]
    TIGRFAMsi TIGR00294. TIGR00294. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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).

    Entry informationi

    Entry nameiGCH4_NITEU
    AccessioniPrimary (citable) accession number: Q82VD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3