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P0A6T5

- GCH1_ECOLI

UniProt

P0A6T5 - GCH1_ECOLI

Protein

GTP cyclohydrolase 1

Gene

folE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Enzyme regulationi

    Allosteric enzyme. Activity is modulated by K+, divalent cations, UTP, and tetrahydrobiopterin. Tetrahydrobiopterin is an inhibitor of this enzyme.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi111 – 1111Zinc
    Metal bindingi114 – 1141Zinc
    Metal bindingi182 – 1821Zinc

    GO - Molecular functioni

    1. GTP binding Source: EcoliWiki
    2. GTP cyclohydrolase I activity Source: EcoCyc
    3. zinc ion binding Source: EcoCyc

    GO - Biological processi

    1. 7,8-dihydroneopterin 3'-triphosphate biosynthetic process Source: UniProtKB-UniPathway
    2. one-carbon metabolic process Source: UniProtKB-HAMAP
    3. queuosine biosynthetic process Source: EcoCyc
    4. tetrahydrofolate biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciEcoCyc:GTP-CYCLOHYDRO-I-MONOMER.
    ECOL316407:JW2140-MONOMER.
    MetaCyc:GTP-CYCLOHYDRO-I-MONOMER.
    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:folE
    Ordered Locus Names:b2153, JW2140
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11375. folE.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoliWiki
    2. protein complex Source: EcoliWiki

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 222221GTP cyclohydrolase 1PRO_0000119404Add
    BLAST

    Proteomic databases

    PaxDbiP0A6T5.
    PRIDEiP0A6T5.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A6T5.

    Interactioni

    Subunit structurei

    Toroid-shaped homodecamer, composed of two pentamers of five dimers.2 Publications

    Protein-protein interaction databases

    BioGridi853284. 1 interaction.
    DIPiDIP-9676N.
    IntActiP0A6T5. 1 interaction.
    MINTiMINT-6732927.
    STRINGi511145.b2153.

    Structurei

    Secondary structure

    1
    222
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 1712
    Helixi33 – 5018
    Helixi58 – 614
    Helixi63 – 7311
    Turni74 – 763
    Helixi77 – 793
    Helixi81 – 833
    Beta strandi89 – 913
    Beta strandi100 – 11112
    Turni112 – 1154
    Beta strandi116 – 12611
    Beta strandi129 – 1335
    Helixi135 – 14612
    Beta strandi147 – 1504
    Helixi152 – 16716
    Beta strandi172 – 1809
    Helixi181 – 1844
    Beta strandi194 – 2007
    Helixi203 – 2064
    Helixi208 – 21710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A8RX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-222[»]
    1A9CX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-222[»]
    1FBXX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-222[»]
    1GTPX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T2-222[»]
    1N3RX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-222[»]
    1N3SX-ray2.55A/B/C/D/E/F/G/H/I/J2-222[»]
    1N3TX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-222[»]
    ProteinModelPortaliP0A6T5.
    SMRiP0A6T5. Positions 2-222.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6T5.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GTP cyclohydrolase I family.Curated

    Phylogenomic databases

    eggNOGiCOG0302.
    HOGENOMiHOG000221222.
    KOiK01495.
    OMAiQRIAEHM.
    OrthoDBiEOG6XHC8G.
    PhylomeDBiP0A6T5.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A6T5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSLSKEAAL VHEALVARGL ETPLRPPVHE MDNETRKSLI AGHMTEIMQL    50
    LNLDLADDSL METPHRIAKM YVDEIFSGLD YANFPKITLI ENKMKVDEMV 100
    TVRDITLTST CEHHFVTIDG KATVAYIPKD SVIGLSKINR IVQFFAQRPQ 150
    VQERLTQQIL IALQTLLGTN NVAVSIDAVH YCVKARGIRD ATSATTTTSL 200
    GGLFKSSQNT RHEFLRAVRH HN 222
    Length:222
    Mass (Da):24,831
    Last modified:January 23, 2007 - v2
    Checksum:i23C6A1440F579FC2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63910 Genomic DNA. Translation: CAA45365.1.
    U00007 Genomic DNA. Translation: AAA60535.1.
    U00096 Genomic DNA. Translation: AAC75214.1.
    AP009048 Genomic DNA. Translation: BAE76630.1.
    PIRiH64983.
    S29895.
    RefSeqiNP_416658.1. NC_000913.3.
    YP_490392.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75214; AAC75214; b2153.
    BAE76630; BAE76630; BAE76630.
    GeneIDi12934530.
    949040.
    KEGGiecj:Y75_p2115.
    eco:b2153.
    PATRICi32119653. VBIEscCol129921_2237.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63910 Genomic DNA. Translation: CAA45365.1 .
    U00007 Genomic DNA. Translation: AAA60535.1 .
    U00096 Genomic DNA. Translation: AAC75214.1 .
    AP009048 Genomic DNA. Translation: BAE76630.1 .
    PIRi H64983.
    S29895.
    RefSeqi NP_416658.1. NC_000913.3.
    YP_490392.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A8R X-ray 2.10 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O 2-222 [» ]
    1A9C X-ray 2.90 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O 2-222 [» ]
    1FBX X-ray 2.80 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O 2-222 [» ]
    1GTP X-ray 3.00 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 2-222 [» ]
    1N3R X-ray 2.80 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O 2-222 [» ]
    1N3S X-ray 2.55 A/B/C/D/E/F/G/H/I/J 2-222 [» ]
    1N3T X-ray 3.20 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O 2-222 [» ]
    ProteinModelPortali P0A6T5.
    SMRi P0A6T5. Positions 2-222.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 853284. 1 interaction.
    DIPi DIP-9676N.
    IntActi P0A6T5. 1 interaction.
    MINTi MINT-6732927.
    STRINGi 511145.b2153.

    Proteomic databases

    PaxDbi P0A6T5.
    PRIDEi P0A6T5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75214 ; AAC75214 ; b2153 .
    BAE76630 ; BAE76630 ; BAE76630 .
    GeneIDi 12934530.
    949040.
    KEGGi ecj:Y75_p2115.
    eco:b2153.
    PATRICi 32119653. VBIEscCol129921_2237.

    Organism-specific databases

    EchoBASEi EB1349.
    EcoGenei EG11375. folE.

    Phylogenomic databases

    eggNOGi COG0302.
    HOGENOMi HOG000221222.
    KOi K01495.
    OMAi QRIAEHM.
    OrthoDBi EOG6XHC8G.
    PhylomeDBi P0A6T5.

    Enzyme and pathway databases

    UniPathwayi UPA00848 ; UER00151 .
    BioCyci EcoCyc:GTP-CYCLOHYDRO-I-MONOMER.
    ECOL316407:JW2140-MONOMER.
    MetaCyc:GTP-CYCLOHYDRO-I-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A6T5.
    PROi P0A6T5.

    Gene expression databases

    Genevestigatori P0A6T5.

    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. "Biosynthesis of tetrahydrofolate. Sequence of GTP cyclohydrolase I from Escherichia coli."
      Katzenmeier G., Schmid C., Kellermann J., Lottspeich F., Bacher A.
      Biol. Chem. Hoppe-Seyler 372:991-997(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: K12.
    2. "Studies on GTP cyclohydrolase I of Escherichia coli."
      Schmid C., Meining W., Weinkauf S., Bachmann L., Ritz H., Eberhardt S., Gimbel W., Werner T., Lahm H.W., Nar H., Bacher A.
      Adv. Exp. Med. Biol. 338:157-162(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. "Automated multiplex sequencing of the E.coli genome."
      Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.
      Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / BHB2600.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Allosteric characteristics of GTP cyclohydrolase I from Escherichia coli."
      Schoedon G., Redweik U., Frank G., Cotton R.G.H., Blau N.
      Eur. J. Biochem. 210:561-568(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-51 AND 99-129, CHARACTERIZATION.
    7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    8. "Biochemical characterization of oligomerization of Escherichia coli GTP cyclohydrolase I."
      Lee S., Ahn C., Park E., Hwang D.S., Yim J.
      J. Biochem. Mol. Biol. 35:255-261(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    10. "Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I."
      Rebelo J., Auerbach G., Bader G., Bracher A., Nar H., Hosl C., Schramek N., Kaiser J., Bacher A., Huber R., Fischer M.
      J. Mol. Biol. 326:503-516(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT SER-113.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT, ZINC-BINDING SITES.

    Entry informationi

    Entry nameiGCH1_ECOLI
    AccessioniPrimary (citable) accession number: P0A6T5
    Secondary accession number(s): P27511, Q2MAS6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 89 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3