ID   GCH1_CHRSD              Reviewed;         184 AA.
AC   Q1QV64;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=Csal_2294;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-2006) 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: 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; CP000285; ABE59644.1; -; Genomic_DNA.
DR   RefSeq; YP_574343.1; -.
DR   GeneID; 4026447; -.
DR   GenomeReviews; CP000285_GR; Csal_2294.
DR   KEGG; csa:Csal_2294; -.
DR   NMPDR; fig|290398.4.peg.1774; -.
DR   HOGENOM; Q1QV64; -.
DR   OMA; Q1QV64; ARIVEMF.
DR   BioCyc; CSAL290398:CSAL_2294-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; 1.
PE   3: Inferred from homology;
KW   Complete proteome; GTP-binding; Hydrolase; Metal-binding;
KW   Nucleotide-binding; One-carbon metabolism; Zinc.
FT   CHAIN         1    184       GTP cyclohydrolase 1.
FT                                /FTId=PRO_1000043676.
FT   METAL        75     75       Zinc (By similarity).
FT   METAL        78     78       Zinc (By similarity).
FT   METAL       146    146       Zinc (By similarity).
SQ   SEQUENCE   184 AA;  20819 MW;  DBFB64887A369721 CRC64;
     MTEELADNYR HIIAGLGEDP DREGLRDTPK RAAKAMQFLT QGYGQTLESL VNGAVFESQT
     DEMVLIKDIE LYSMCEHHLL PFIGKCHIAY LPEGRVLGLS KFARIVDMYA RRMQIQENLT
     RQIAEAVQQV TQARGVGVII EAQHMCMMMR GVEKQNSSMK TSVMLGAFRN NLTTRQEFLT
     LVHG
//