ID   GCH1_DEHE1              Reviewed;         189 AA.
AC   Q3Z782;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=DET1204;
OS   Dehalococcoides ethenogenes (strain 195).
OC   Bacteria; Chloroflexi; Dehalococcoidetes; Dehalococcoides.
OX   NCBI_TaxID=243164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15637277; DOI=10.1126/science.1102226;
RA   Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M.,
RA   Methe B.A., Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M.,
RA   Kolonay J.F., Dodson R.J., Daugherty S.C., Brinkac L.M.,
RA   Sullivan S.A., Madupu R., Nelson K.E., Kang K.H., Impraim M., Tran K.,
RA   Robinson J.M., Forberger H.A., Fraser C.M., Zinder S.H.,
RA   Heidelberg J.F.;
RT   "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT   ethenogenes.";
RL   Science 307:105-108(2005).
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: Toroid-shaped homodecamer, composed of two pentamers of
CC       five dimers (By similarity).
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family.
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DR   EMBL; CP000027; AAW39542.1; -; Genomic_DNA.
DR   RefSeq; YP_181917.1; -.
DR   GeneID; 3229503; -.
DR   GenomeReviews; CP000027_GR; DET1204.
DR   KEGG; det:DET1204; -.
DR   NMPDR; fig|243164.3.peg.1106; -.
DR   TIGR; DET1204; -.
DR   HOGENOM; Q3Z782; -.
DR   OMA; Q3Z782; ARIVEMF.
DR   BioCyc; DETH243164:DET_1204-MON; -.
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    189       GTP cyclohydrolase 1.
FT                                /FTId=PRO_1000043687.
FT   METAL        76     76       Zinc (By similarity).
FT   METAL        79     79       Zinc (By similarity).
FT   METAL       149    149       Zinc (By similarity).
SQ   SEQUENCE   189 AA;  21170 MW;  CC03BE97DE462B0C CRC64;
     MFDEQAIKQS VQNMLLAIGE DPEREGLKET PRRVAQMYAE LFSGMNQDPA EVLRVGYELG
     HREMVIIKDI PFYSMCEHHL LPFSGVVHIG YIPNIDGRVV GISKLARVVE IYAKRPQIQE
     RMATQIADAI IDGLKCDGVA VVIEAEHMCM VMRGIKKPGS RVITSALRGS FHKSPAARAE
     FLSLIQQKH
//