GCH1_CAMJE
ID GCH1_CAMJE Reviewed; 190 AA.
AC P51594; Q0PBU5; Q9PIT5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 122.
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=Cj0194;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=7670637; DOI=10.1099/13500872-141-6-1359;
RA Griffiths P.L., Park R.W.A., Connerton I.F.;
RT "The gene for Campylobacter trigger factor: evidence for multiple
RT transcription start sites and protein products.";
RL Microbiology 141:1359-1367(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA59929.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X85954; CAA59929.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL111168; CAL34363.1; -; Genomic_DNA.
DR PIR; A81438; A81438.
DR PIR; I40754; I40754.
DR RefSeq; WP_002851990.1; NC_002163.1.
DR RefSeq; YP_002343652.1; NC_002163.1.
DR AlphaFoldDB; P51594; -.
DR SMR; P51594; -.
DR IntAct; P51594; 1.
DR STRING; 192222.Cj0194; -.
DR PaxDb; P51594; -.
DR PRIDE; P51594; -.
DR EnsemblBacteria; CAL34363; CAL34363; Cj0194.
DR GeneID; 904536; -.
DR KEGG; cje:Cj0194; -.
DR PATRIC; fig|192222.6.peg.191; -.
DR eggNOG; COG0302; Bacteria.
DR HOGENOM; CLU_049768_3_1_7; -.
DR OMA; CEHMCMS; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000000799; 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.
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_0000119393"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 190 AA; 21800 MW; 24B4CC39BEA49564 CRC64;
MQKKFEDCVK TMLEIIGENP NREGLIKTPN RVFKAYEFLT SGYTQNVKEI LNDALFESSN
NEMVLVRDIE FYSLCEHHLL PFFGRAHVAY IPNKKVVGLS KIPRLVEVFA RRLQIQEQLT
EQIAQALMEN VDAKGVGVVI EARHMCVEMR GVQKANSTTT TSALRGIFLK NEKTREEFFS
LINSAKQVRF
