GCH1_RICPR
ID GCH1_RICPR Reviewed; 190 AA.
AC Q9ZDE8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=RP383;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate +
CC H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:58462; EC=3.5.4.16;
CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC -!- SUBUNIT: Toroid-shaped homodecamer, composed of two pentamers of five
CC dimers. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. {ECO:0000305}.
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DR EMBL; AJ235271; CAA14840.1; -; Genomic_DNA.
DR PIR; F71695; F71695.
DR RefSeq; NP_220764.1; NC_000963.1.
DR RefSeq; WP_004597557.1; NC_000963.1.
DR AlphaFoldDB; Q9ZDE8; -.
DR SMR; Q9ZDE8; -.
DR STRING; 272947.RP383; -.
DR EnsemblBacteria; CAA14840; CAA14840; CAA14840.
DR GeneID; 57569507; -.
DR KEGG; rpr:RP383; -.
DR PATRIC; fig|272947.5.peg.393; -.
DR eggNOG; COG0302; Bacteria.
DR HOGENOM; CLU_049768_3_1_5; -.
DR OMA; YHETIYD; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000002480; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.286.10; -; 1.
DR Gene3D; 3.30.1130.10; -; 1.
DR HAMAP; MF_00223; FolE; 1.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR InterPro; IPR043134; GTP-CH-I_N.
DR InterPro; IPR001474; GTP_CycHdrlase_I.
DR InterPro; IPR018234; GTP_CycHdrlase_I_CS.
DR InterPro; IPR020602; GTP_CycHdrlase_I_dom.
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 GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW One-carbon metabolism; Reference proteome; Zinc.
FT CHAIN 1..190
FT /note="GTP cyclohydrolase 1"
FT /id="PRO_0000119439"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 190 AA; 21790 MW; B7F89C89D5337A38 CRC64;
MSKPTREEAK EAVRTLLKFI GEDPNREGLL KTPDRVINSY TEIFSGYGKD AQEILNTKFY
DICNFQDLIS LEGIKFTSFC EHHILPFNGT VHIAYIPDNC IIGVSKLARI VNIFARRLQI
QEKMTLEIAE SVQENLKPLG VAVKISALHS CMSMRGVMHD NSVMNTMYYT GIFAEQQKYR
YEFLNLIAKR
