ID   GCH1_BAUCH              Reviewed;         220 AA.
AC   Q1LT77;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=BCI_0394;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000238; ABF13956.1; -; Genomic_DNA.
DR   RefSeq; YP_588837.1; -.
DR   GeneID; 4056702; -.
DR   GenomeReviews; CP000238_GR; BCI_0394.
DR   KEGG; bci:BCI_0394; -.
DR   HOGENOM; Q1LT77; -.
DR   OMA; Q1LT77; YLPRKNI.
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    220       GTP cyclohydrolase 1.
FT                                /FTId=PRO_1000043667.
FT   METAL       110    110       Zinc (By similarity).
FT   METAL       113    113       Zinc (By similarity).
FT   METAL       181    181       Zinc (By similarity).
SQ   SEQUENCE   220 AA;  24802 MW;  8A7E971B06DAB2D3 CRC64;
     MVILTKEASM VRQALLANGL EPFLRGEERL GIEARKRRIA AHMKKIMTLL NLDLADDSLA
     KTPYRIAYMY IEEIFPGLDY ANFPQITLIS NKMKADEMVT VRNITLTSTC EHHFLMIDGK
     ATVSYIPKSN VIGLSKINRI VRFFAQRPQV QERLTQQILL ALQTILGTNN VAVSIYAVHY
     CVKARGICDS TSTTTTTSLG GIFKSSQNTR QEFLRTINQT
//