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P19465

- GCH1_BACSU

UniProt

P19465 - GCH1_BACSU

Protein

GTP cyclohydrolase 1

Gene

folE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      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

    K+ ions moderately increases the Vmax, whereas UTP and Ca2+ and Mg2+ ions drastically increase the Km for GTP.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi78 – 781ZincBy similarity
    Metal bindingi81 – 811ZincBy similarity
    Metal bindingi150 – 1501ZincBy similarity

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. GTP cyclohydrolase I activity Source: UniProtKB-HAMAP
    3. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

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

    BioCyciBSUB:BSU22780-MONOMER.
    MetaCyc:BSU22780-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
    Synonyms:mtrA
    Ordered Locus Names:BSU22780
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU22780. [Micado]

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 190190GTP cyclohydrolase 1PRO_0000119386Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi224308.BSU22780.

    Structurei

    3D structure databases

    ProteinModelPortaliP19465.
    SMRiP19465. Positions 2-188.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GTP cyclohydrolase I family.Curated

    Phylogenomic databases

    HOGENOMiHOG000221222.
    KOiK01495.
    OMAiYEQIEYA.
    OrthoDBiEOG6XHC8G.
    PhylomeDBiP19465.

    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.

    P19465-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKEVNKEQIE QAVRQILEAI GEDPNREGLL DTPKRVAKMY AEVFSGLNED    50
    PKEHFQTIFG ENHEELVLVK DIAFHSMCEH HLVPFYGKAH VAYIPRGGKV 100
    TGLSKLARAV EAVAKRPQLQ ERITSTIAES IVETLDPHGV MVVVEAEHMC 150
    MTMRGVRKPG AKTVTSAVRG VFKDDAAARA EVLEHIKRQD 190
    Length:190
    Mass (Da):21,219
    Last modified:February 1, 1991 - v1
    Checksum:iE912535CC67A5551
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37320 Genomic DNA. Translation: AAA22615.1.
    M80245 Genomic DNA. Translation: AAA20852.1.
    AL009126 Genomic DNA. Translation: CAB14194.1.
    X52418 Genomic DNA. No translation available.
    PIRiA38256.
    RefSeqiNP_390159.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB14194; CAB14194; BSU22780.
    GeneIDi938994.
    KEGGibsu:BSU22780.
    PATRICi18976367. VBIBacSub10457_2374.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37320 Genomic DNA. Translation: AAA22615.1 .
    M80245 Genomic DNA. Translation: AAA20852.1 .
    AL009126 Genomic DNA. Translation: CAB14194.1 .
    X52418 Genomic DNA. No translation available.
    PIRi A38256.
    RefSeqi NP_390159.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P19465.
    SMRi P19465. Positions 2-188.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU22780.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14194 ; CAB14194 ; BSU22780 .
    GeneIDi 938994.
    KEGGi bsu:BSU22780.
    PATRICi 18976367. VBIBacSub10457_2374.

    Organism-specific databases

    GenoListi BSU22780. [Micado ]

    Phylogenomic databases

    HOGENOMi HOG000221222.
    KOi K01495.
    OMAi YEQIEYA.
    OrthoDBi EOG6XHC8G.
    PhylomeDBi P19465.

    Enzyme and pathway databases

    UniPathwayi UPA00848 ; UER00151 .
    BioCyci BSUB:BSU22780-MONOMER.
    MetaCyc:BSU22780-MONOMER.

    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. "The mtr locus is a two-gene operon required for transcription attenuation in the trp operon of Bacillus subtilis."
      Gollnick P., Ishino S., Kuroda M.I., Henner D.J., Yanofsky C.
      Proc. Natl. Acad. Sci. U.S.A. 87:8726-8730(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "Molecular cloning, nucleotide sequence, and characterization of the Bacillus subtilis gene encoding the DNA-binding protein HBsu."
      Micka B., Groch N., Heinemann U., Marahiel M.A.
      J. Bacteriol. 173:3191-3198(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
      Strain: 168 / JH642.
    4. "The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis."
      Babitzke P., Gollnick P., Yanofsky C.
      J. Bacteriol. 174:2059-2064(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Enzymic characterization of Bacillus subtilis GTP cyclohydrolase I. Evidence for a chemical dephosphorylation of dihydroneopterin triphosphate."
      de Saizieu A., Vankan P., van Loon A.P.
      Biochem. J. 306:371-377(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.

    Entry informationi

    Entry nameiGCH1_BACSU
    AccessioniPrimary (citable) accession number: P19465
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 111 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

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3