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Q5F9K6

- GCH4_NEIG1

UniProt

Q5F9K6 - GCH4_NEIG1

Protein

GTP cyclohydrolase FolE2

Gene

folE2

Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (15 Mar 2005)
      Previous versions | rss
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    Functioni

    Converts GTP to 7,8-dihydroneopterin triphosphate.1 Publication

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei147 – 1471May be catalytically importantBy 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

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciNGON242231:GI2G-366-MONOMER.
    UniPathwayiUPA00848; UER00151.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTP cyclohydrolase FolE2 (EC:3.5.4.16)
    Alternative name(s):
    GTP cyclohydrolase 1B
    Gene namesi
    Name:folE2
    Ordered Locus Names:NGO0387
    OrganismiNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
    Taxonomic identifieri242231 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
    ProteomesiUP000000535: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 257257GTP cyclohydrolase FolE2PRO_0000147714Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi242231.NGO0387.

    Structurei

    Secondary structure

    1
    257
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 3417
    Beta strandi37 – 5115
    Helixi61 – 699
    Helixi76 – 8914
    Beta strandi93 – 10816
    Turni110 – 1123
    Beta strandi115 – 12915
    Beta strandi132 – 14615
    Helixi148 – 1536
    Beta strandi154 – 1563
    Beta strandi160 – 17314
    Helixi177 – 1859
    Beta strandi188 – 1914
    Helixi198 – 21013
    Helixi215 – 22814
    Beta strandi232 – 24110
    Beta strandi246 – 25611

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3D1TX-ray2.20A/B1-257[»]
    3D2OX-ray2.04A/B1-257[»]
    ProteinModelPortaliQ5F9K6.
    SMRiQ5F9K6. Positions 15-256.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5F9K6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GTP cyclohydrolase IV family.Curated

    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]
    TIGRFAMsiTIGR00294. TIGR00294. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q5F9K6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNAIADVQSS RDLRNLPINQ VGIKDLRFPI TLKTAEGTQS TVARLTMTVY    50
    LPAEQKGTHM SRFVALMEQH TEVLDFAQLH RLTAEMVALL DSRAGKISVS 100
    FPFFRKKTAP VSGIRSLLDY DVSLTGEMKD GAYGHSMKVM IPVTSLCPCS 150
    KEISQYGAHN QRSHVTVSLT SDAEVGIEEV IDYVETQASC QLYGLLKRPD 200
    EKYVTEKAYE NPKFVEDMVR DVATSLIADK RIKSFVVESE NFESIHNHSA 250
    YAYIAYP 257
    Length:257
    Mass (Da):28,747
    Last modified:March 15, 2005 - v1
    Checksum:iA0235399C3EDF2A9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004969 Genomic DNA. Translation: AAW89131.1.
    RefSeqiYP_207543.1. NC_002946.2.

    Genome annotation databases

    EnsemblBacteriaiAAW89131; AAW89131; NGO0387.
    GeneIDi3282560.
    KEGGingo:NGO0387.
    PATRICi20333781. VBINeiGon24812_0468.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004969 Genomic DNA. Translation: AAW89131.1 .
    RefSeqi YP_207543.1. NC_002946.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3D1T X-ray 2.20 A/B 1-257 [» ]
    3D2O X-ray 2.04 A/B 1-257 [» ]
    ProteinModelPortali Q5F9K6.
    SMRi Q5F9K6. Positions 15-256.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 242231.NGO0387.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAW89131 ; AAW89131 ; NGO0387 .
    GeneIDi 3282560.
    KEGGi ngo:NGO0387.
    PATRICi 20333781. VBINeiGon24812_0468.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00848 ; UER00151 .
    BioCyci NGON242231:GI2G-366-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q5F9K6.

    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. "The complete genome sequence of Neisseria gonorrhoeae."
      Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H.
      , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700825 / FA 1090.
    2. Cited for: FUNCTION, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiGCH4_NEIG1
    AccessioniPrimary (citable) accession number: Q5F9K6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2005
    Last sequence update: March 15, 2005
    Last modified: October 1, 2014
    This is version 57 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