ID GCH1_BACCR Reviewed; 189 AA.
AC Q81FQ8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 01-MAY-2013, entry version 72.
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=BC_1511;
OS Bacillus cereus (strain ATCC 14579 / DSM 31).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B.,
RA Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A.,
RA Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T.,
RA Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D.,
RA Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with
RT Bacillus anthracis.";
RL Nature 423:87-91(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; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin 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; AE016877; AAP08491.1; -; Genomic_DNA.
DR RefSeq; NP_831290.1; NC_004722.1.
DR ProteinModelPortal; Q81FQ8; -.
DR STRING; 226900.BC1511; -.
DR EnsemblBacteria; AAP08491; AAP08491; BC_1511.
DR GeneID; 1203860; -.
DR KEGG; bce:BC1511; -.
DR PATRIC; 32598758; VBIBacCer54481_1488.
DR eggNOG; COG0302; -.
DR KO; K01495; -.
DR OMA; LIRHQPA; -.
DR ProtClustDB; PRK09347; -.
DR BioCyc; BCER226900:GJEU-1511-MONOMER; -.
DR UniPathway; UPA00848; UER00151.
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:HAMAP.
DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:HAMAP.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:HAMAP.
DR HAMAP; MF_00223; FolE; 1; -.
DR InterPro; IPR001474; GTP_CycHdrlase_I.
DR InterPro; IPR020602; GTP_CycHdrlase_I/CN_OxRdtase.
DR InterPro; IPR018234; GTP_CycHdrlase_I_CS.
DR PANTHER; PTHR11109; PTHR11109; 1.
DR Pfam; PF01227; 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; Reference proteome; Zinc.
FT CHAIN 1 189 GTP cyclohydrolase 1.
FT /FTId=PRO_0000119383.
FT METAL 78 78 Zinc (By similarity).
FT METAL 81 81 Zinc (By similarity).
FT METAL 150 150 Zinc (By similarity).
SQ SEQUENCE 189 AA; 21020 MW; 0A8B0379657B322B CRC64;
MAKVNLEQIE HAVRLILEAI GDDPNREGVL DTPKRVAKMY AEVFSGMHED PKEHLHKVFG
EDHEELVLVK DIPFYSMCEH HLVPFYGVAH VAYIPQGGKV TGLSKLARTV DTIARRPQLQ
ERITSTVANS IMEVLEPHGV MVVVEAEHMC MTMRGVKKPG AKTVTTAVRG VLENDAAARS
EILSFIKTK
//
