ID   GCH1_COXBU              Reviewed;         184 AA.
AC   Q83DE3;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 45.
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=CBU_0795;
OS   Coxiella burnetii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Coxiellaceae; Coxiella.
OX   NCBI_TaxID=777;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nine Mile phase I / RSA 493;
RX   MEDLINE=22608657; PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E.,
RA   Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J.,
RA   DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J.,
RA   Khouri H.M., Lee K.H., Carty H.A., Scanlan D., Heinzen R.A.,
RA   Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella
RT   burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO90329.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_819815.2; -.
DR   HSSP; P22288; 1IS8.
DR   GeneID; 1208688; -.
DR   GenomeReviews; AE016828_GR; CBU_0795.
DR   KEGG; cbu:CBU_0795; -.
DR   NMPDR; fig|227377.1.peg.759; -.
DR   TIGR; CBU_0795; -.
DR   HOGENOM; Q83DE3; -.
DR   OMA; Q83DE3; ARIVEMF.
DR   BioCyc; CBUR227377:CBU_0795-MON; -.
DR   BRENDA; 3.5.4.16; 256353.
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_0000119402.
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;  20777 MW;  C69EA3EA9C15ABA4 CRC64;
     MSNTIADHVK AILIALGEDP NREGLRDTPK RYEKALEHLT KGYHEKLPSV VKKAVFQSGM
     DEMVILKDIE LYSLCEHHLL PFIGRCHVAY LPSGKIIGIS KLARIVDMFA KRLQVQENLT
     KQIAEAILTA TEAKGVGVII EAKHLCMMMR GVEKQNSEMT TSVMLGTFRK DDRTRSEFLS
     LIRK
//