ID   GCH1_BRUC2              Reviewed;         213 AA.
AC   A9M586;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   22-JUL-2008, entry version 7.
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=BCAN_A1090;
OS   Brucella canis (strain ATCC 23365 / NCTC 10854).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=483179;
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 canis ATCC 23365 whole genome shotgun sequencing project.";
RL   Submitted (OCT-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; CP000872; ABX62141.1; -; Genomic_DNA.
DR   RefSeq; YP_001592912.1; -.
DR   GeneID; 5784077; -.
DR   GenomeReviews; CP000872_GR; BCAN_A1090.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:HAMAP.
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_CycOHase_I.
DR   PANTHER; PTHR11109; GTP_cyclohydro_I; 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; Hydrolase; Metal-binding; One-carbon metabolism;
KW   Zinc.
FT   CHAIN         1    213       GTP cyclohydrolase 1.
FT                                /FTId=PRO_1000078135.
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;  23794 MW;  B43866DF2C208BB5 CRC64;
     MDARILQDND DTSLPVNQAS VTRIHKKPGK AEAEAAVRTL LLWAGEDPDR EGLLETPKRV
     AKAYQELFGG YSESPEEVLG TTFEEVAGYD DMVLVKDISF FSHCEHHMVP IIGKAHVAYL
     PEGRVVGLSK IARVVDIFAR RLQTQESITA QIADSMQRIL KPRGVAVMIE AEHMCMAMRS
     IRKQGSSTIT TTFTGDFKEK ADQQVRFMTL IRT
//