Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P51599

- GCH1_NEUCR

UniProt

P51599 - GCH1_NEUCR

Protein

GTP cyclohydrolase 1

Gene

gch-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (30 Apr 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 bindingi202 – 2021ZincBy similarity
    Metal bindingi205 – 2051ZincBy similarity
    Metal bindingi273 – 2731ZincBy 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
    Gene namesi
    Name:gch-1
    ORF Names:104H10.80, NCU07774
    OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
    Taxonomic identifieri367110 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
    ProteomesiUP000001805: Chromosome 2, Linkage Group V

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 313313GTP cyclohydrolase 1PRO_0000119486Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi5141.NCU07774.1.

    Structurei

    3D structure databases

    ProteinModelPortaliP51599.
    SMRiP51599. Positions 124-310.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GTP cyclohydrolase I family.Curated

    Phylogenomic databases

    eggNOGiCOG0302.
    HOGENOMiHOG000221222.
    KOiK01495.
    OrthoDBiEOG7QRR5W.

    Family and domain databases

    HAMAPiMF_00223. FolE.
    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]
    TIGRFAMsiTIGR00063. folE. 1 hit.
    PROSITEiPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
    PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P51599-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQETTRDGS DSPSGSVSPP IANGTNNKKD KKSSKKRAHS SGERRSSVSK    50
    PARDPSDKPE ESPSKKKKRK TTSSTAAAAV PSTITEEVSP STSVTRSPSP 100
    VIDFDGLSRP SRGTRERLEE TEAQKQERLD KMKGAVRTLL ECIGEDPDRE 150
    GLLATPERYA KAMLFLTKGY QENVRDIVNG AIFQEGHNEM VIVKDIEVFS 200
    MCEHHLVPFT GKMHIGYIPS NAVIGISKLP RIAELFARRL QIQERLTKEV 250
    ANAIMEILKP QGVAVVMESS HLCMVMRGVQ KTTSSTITSC VLGCFESREK 300
    TRLEFLSLIG VNR 313
    Length:313
    Mass (Da):34,471
    Last modified:April 30, 2003 - v2
    Checksum:iC8535C0A7FF84114
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti186 – 1883GHN → DHD in CAA89828. (PubMed:7542887)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL513410 Genomic DNA. Translation: CAC28574.1.
    CM002240 Genomic DNA. Translation: EAA29459.3.
    Z49758 mRNA. Translation: CAA89828.1.
    RefSeqiXP_958695.2. XM_953602.2.

    Genome annotation databases

    EnsemblFungiiEFNCRT00000007952; EFNCRP00000007941; EFNCRG00000007940.
    GeneIDi3874842.
    KEGGincr:NCU07774.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL513410 Genomic DNA. Translation: CAC28574.1 .
    CM002240 Genomic DNA. Translation: EAA29459.3 .
    Z49758 mRNA. Translation: CAA89828.1 .
    RefSeqi XP_958695.2. XM_953602.2.

    3D structure databases

    ProteinModelPortali P51599.
    SMRi P51599. Positions 124-310.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5141.NCU07774.1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EFNCRT00000007952 ; EFNCRP00000007941 ; EFNCRG00000007940 .
    GeneIDi 3874842.
    KEGGi ncr:NCU07774.

    Phylogenomic databases

    eggNOGi COG0302.
    HOGENOMi HOG000221222.
    KOi K01495.
    OrthoDBi EOG7QRR5W.

    Enzyme and pathway databases

    UniPathwayi UPA00848 ; UER00151 .

    Family and domain databases

    HAMAPi MF_00223. FolE.
    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 ]
    TIGRFAMsi TIGR00063. folE. 1 hit.
    PROSITEi PS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
    PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
      Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
      Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
    2. "The genome sequence of the filamentous fungus Neurospora crassa."
      Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
      , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
      Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
    3. "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] OF 185-278.
      Strain: BD AL-2.

    Entry informationi

    Entry nameiGCH1_NEUCR
    AccessioniPrimary (citable) accession number: P51599
    Secondary accession number(s): Q7RV90, Q9C2R6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: April 30, 2003
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3