ID   GCH1_BRUSI              Reviewed;         213 AA.
AC   B0CGM4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   16-JUN-2009, entry version 12.
DE   RecName: Full=GTP cyclohydrolase 1;
DE            EC=3.5.4.16;
DE   AltName: Full=GTP cyclohydrolase I;
DE            Short=GTP-CH-I;
GN   Name=folE; OrderedLocusNames=BSUIS_A1119;
OS   Brucella suis (strain ATCC 23445 / NCTC 10510).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=470137;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J.,
RA   Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S.,
RA   Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K.,
RA   Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W.,
RA   Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C.,
RA   Munk C., Brettin T.S.;
RT   "Brucella suis ATCC 23445 whole genome shotgun sequencing project.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: GTP + H(2)O = formate + 2-amino-4-hydroxy-6-
CC       (erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.
CC   -!- PATHWAY: Cofactor biosynthesis; dihydroneopterin triphosphate
CC       biosynthesis; 2-amino-4-hydroxy-6-(erythro-1,2,3-
CC       trihydroxypropyl)-dihydropteridine triphosphate from GTP: step
CC       1/1.
CC   -!- SUBUNIT: Homopolymer (By similarity).
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family.
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DR   EMBL; CP000911; ABY38175.1; -; Genomic_DNA.
DR   RefSeq; YP_001627745.1; -.
DR   GeneID; 5837474; -.
DR   GenomeReviews; CP000911_GR; BSUIS_A1119.
DR   KEGG; bmt:BSUIS_A1119; -.
DR   OMA; B0CGM4; ARIVEMF.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IEA:HAMAP.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00223; -; 1.
DR   InterPro; IPR001474; GTP_CycHdrlase_I.
DR   InterPro; IPR018234; GTP_CycHdrlase_I_CS.
DR   PANTHER; PTHR11109; GTP_cyclohydro_I; 1.
DR   Pfam; PF01227; GTP_cyclohydroI; 1.
DR   ProDom; PD003330; GTP_cyclohydroI; 1.
DR   TIGRFAMs; TIGR00063; folE; 1.
DR   PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
DR   PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; GTP-binding; Hydrolase; Metal-binding;
KW   Nucleotide-binding; One-carbon metabolism; Zinc.
FT   CHAIN         1    213       GTP cyclohydrolase 1.
FT                                /FTId=PRO_1000078136.
FT   METAL       104    104       Zinc (By similarity).
FT   METAL       107    107       Zinc (By similarity).
FT   METAL       175    175       Zinc (By similarity).
SQ   SEQUENCE   213 AA;  23802 MW;  EF96D97E2835871E CRC64;
     MDARILQDND DTSLPVNQAS VTRIHKKPGK PEAEAAVRTL LLWAGEDPDR EGLLETPKRV
     AKAYQELFGG YSESPEEVLG TTFEEVAGYD DMVLVKDISF FSHCEHHMVP IIGKAHVAYL
     PEGRVVGLSK IARVVDIFAR RLQTQESITA QIADSIQRIL KPRGVAVMIE AEHMCMAMRS
     IRKQGSSTIT TTFTGDFKEK ADQQVRFMTL IRT
//