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P94398

- GCH4_BACSU

UniProt

P94398 - GCH4_BACSU

Protein

GTP cyclohydrolase FolE2

Gene

folE2

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 83 (01 Oct 2014)
      Sequence version 2 (16 Jun 2009)
      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
    Sitei183 – 1831May 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

    BioCyciBSUB:BSU03340-MONOMER.
    UniPathwayiUPA00848; UER00151.

    Protein family/group databases

    TCDBi9.B.10.1.1. the putative tripartite zn(2+) transporter (tzt) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTP cyclohydrolase FolE2 (EC:3.5.4.16)
    Alternative name(s):
    GTP cyclohydrolase 1B
    Gene namesi
    Name:folE2
    Synonyms:yciA
    Ordered Locus Names:BSU03340
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU03340. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 304304GTP cyclohydrolase FolE2PRO_0000147701Add
    BLAST

    Proteomic databases

    PaxDbiP94398.

    Expressioni

    Inductioni

    Repressed by zinc, via zur.1 Publication

    Interactioni

    Protein-protein interaction databases

    IntActiP94398. 1 interaction.
    MINTiMINT-8366745.
    STRINGi224308.BSU03340.

    Structurei

    3D structure databases

    ProteinModelPortaliP94398.
    SMRiP94398. Positions 44-298.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GTP cyclohydrolase IV family.Curated

    Phylogenomic databases

    eggNOGiCOG1469.
    HOGENOMiHOG000280679.
    KOiK09007.
    OrthoDBiEOG6X6RBH.
    PhylomeDBiP94398.

    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.

    P94398-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNQHTLLPKK TERLQYFGSV SPIKGEKPVE KEKMKDLQNI RKDYFFDIQH    50
    VGVANVSHPV TITSAMMPAE QTTAANFTMT CNLPRNQKGI NMSRLTELLQ 100
    VYHQNGWILS FSSLQQFTKE LAENMDTSSA TVEVRFPWFF ERKSPKLEKA 150
    GLMHADIFMS VTYRKDQPFK QRAGISAKVT TLCPCSKEIS EYSAHNQRGT 200
    VSIWADIHPA ASLPSDVKAD LLHAAESNAS ARLHPVLKRP DEKAVTETAY 250
    ENPRFVEDLA RLIAADLFEL EWVSAFEIEC RNEESIHLHD AYAKLCFSKE 300
    VDKI 304
    Length:304
    Mass (Da):34,564
    Last modified:June 16, 2009 - v2
    Checksum:i90A28F90FE9BDAB3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti202 – 2098SIWADIHP → KHLGRIFTR in BAA08968. (PubMed:8969502)Curated
    Sequence conflicti222 – 2221L → P in BAA08968. (PubMed:8969502)Curated
    Sequence conflicti290 – 2956DAYAKL → RCLCEV in BAA08968. (PubMed:8969502)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50453 Genomic DNA. Translation: BAA08968.1.
    AL009126 Genomic DNA. Translation: CAB12128.2.
    PIRiH69759.
    RefSeqiNP_388216.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12128; CAB12128; BSU03340.
    GeneIDi938325.
    KEGGibsu:BSU03340.
    PATRICi18972227. VBIBacSub10457_0342.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50453 Genomic DNA. Translation: BAA08968.1 .
    AL009126 Genomic DNA. Translation: CAB12128.2 .
    PIRi H69759.
    RefSeqi NP_388216.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali P94398.
    SMRi P94398. Positions 44-298.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P94398. 1 interaction.
    MINTi MINT-8366745.
    STRINGi 224308.BSU03340.

    Protein family/group databases

    TCDBi 9.B.10.1.1. the putative tripartite zn(2+) transporter (tzt) family.

    Proteomic databases

    PaxDbi P94398.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12128 ; CAB12128 ; BSU03340 .
    GeneIDi 938325.
    KEGGi bsu:BSU03340.
    PATRICi 18972227. VBIBacSub10457_0342.

    Organism-specific databases

    GenoListi BSU03340. [Micado ]

    Phylogenomic databases

    eggNOGi COG1469.
    HOGENOMi HOG000280679.
    KOi K09007.
    OrthoDBi EOG6X6RBH.
    PhylomeDBi P94398.

    Enzyme and pathway databases

    UniPathwayi UPA00848 ; UER00151 .
    BioCyci BSUB:BSU03340-MONOMER.

    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 25 degrees-36 degrees region of the Bacillus subtilis chromosome: determination of the sequence of a 146 kb segment and identification of 113 genes."
      Yamane K., Kumano M., Kurita K.
      Microbiology 142:3047-3056(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    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. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 202-209; 222 AND 290-295.
    4. "Functional analysis of the Bacillus subtilis Zur regulon."
      Gaballa A., Wang T., Ye R.W., Helmann J.D.
      J. Bacteriol. 184:6508-6514(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
      Strain: 168.
    5. Cited for: FUNCTION, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiGCH4_BACSU
    AccessioniPrimary (citable) accession number: P94398
    Secondary accession number(s): Q797Q1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 83 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally thought to be a zinc uptake system.1 Publication

    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