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P51600

- GCH1_PHYBL

UniProt

P51600 - GCH1_PHYBL

Protein

GTP cyclohydrolase 1

Gene
N/A
Organism
Phycomyces blakesleeanus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
  1. Functioni

    GTP cyclohydrolase 1 is the first enzyme in the biosynthetic pathway leading to folic acid.

    Catalytic activityi

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

    Enzyme regulationi

    GTP shows a positive allosteric effect, and tetrahydrobiopterin inhibits the enzyme activity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi18 – 181ZincBy similarity
    Metal bindingi21 – 211ZincBy similarity
    Metal bindingi89 – 891ZincBy similarity

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. GTP cyclohydrolase I activity Source: UniProtKB-EC
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. 7,8-dihydroneopterin 3'-triphosphate biosynthetic process Source: UniProtKB-UniPathway
    2. folic acid biosynthetic process Source: UniProtKB-KW
    3. tetrahydrofolate biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Folate biosynthesis

    Keywords - Ligandi

    GTP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00848; UER00151.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTP cyclohydrolase 1 (EC:3.5.4.16)
    Alternative name(s):
    GTP cyclohydrolase I
    Short name:
    GTP-CH-I
    OrganismiPhycomyces blakesleeanus
    Taxonomic identifieri4837 [NCBI]
    Taxonomic lineageiEukaryotaFungiFungi incertae sedisEarly diverging fungal lineagesMucoromycotinaMucoralesPhycomycetaceaePhycomyces

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›94›94GTP cyclohydrolase 1PRO_0000119487Add
    BLAST

    Interactioni

    Subunit structurei

    Toroid-shaped homodecamer, composed of two pentamers of five dimers.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP51600.
    SMRiP51600. Positions 1-94.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GTP cyclohydrolase I family.Curated

    Family and domain databases

    InterProiIPR001474. GTP_CycHdrlase_I.
    IPR018234. GTP_CycHdrlase_I_CS.
    IPR020602. GTP_CycHdrlase_I_dom.
    [Graphical view]
    PANTHERiPTHR11109. PTHR11109. 1 hit.
    PfamiPF01227. GTP_cyclohydroI. 1 hit.
    [Graphical view]
    PROSITEiPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
    PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    P51600-1 [UniParc]FASTAAdd to Basket

    « Hide

    EDHDEMVIVK DVDIFSLCEH HKVPSTGKIS IGYIPNRRVV GLSKLARIAE   50
    MFSRRLQVQE RLTKQVATAL MEILQPQGVA VVVECSHLCM VMRG 94
    Length:94
    Mass (Da):10,586
    Last modified:October 1, 1996 - v1
    Checksum:i4F8C12A0407A65DD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-terminal residuei94 – 941

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49760 mRNA. Translation: CAA89830.1.
    PIRiS54910.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49760 mRNA. Translation: CAA89830.1 .
    PIRi S54910.

    3D structure databases

    ProteinModelPortali P51600.
    SMRi P51600. Positions 1-94.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00848 ; UER00151 .

    Family and domain databases

    InterProi IPR001474. GTP_CycHdrlase_I.
    IPR018234. GTP_CycHdrlase_I_CS.
    IPR020602. GTP_CycHdrlase_I_dom.
    [Graphical view ]
    PANTHERi PTHR11109. PTHR11109. 1 hit.
    Pfami PF01227. GTP_cyclohydroI. 1 hit.
    [Graphical view ]
    PROSITEi PS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
    PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Homology cloning of GTP-cyclohydrolase I from various unrelated eukaryotes by reverse-transcription polymerase chain reaction using a general set of degenerate primers."
      Maier J., Witter K., Guetlich M., Ziegler I., Werner T., Ninnemann H.
      Biochem. Biophys. Res. Commun. 212:705-711(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: CBS 283.35.

    Entry informationi

    Entry nameiGCH1_PHYBL
    AccessioniPrimary (citable) accession number: P51600
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 65 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3