GCH1_ECO57
ID GCH1_ECO57 Reviewed; 222 AA.
AC P0A6T7; P27511;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 102.
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=Z3409, ECs3045;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG57291.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36468.1; -; Genomic_DNA.
DR PIR; E91009; E91009.
DR PIR; G85853; G85853.
DR RefSeq; NP_311072.1; NC_002695.1.
DR RefSeq; WP_001139613.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A6T7; -.
DR SMR; P0A6T7; -.
DR STRING; 155864.EDL933_3316; -.
DR EnsemblBacteria; AAG57291; AAG57291; Z3409.
DR EnsemblBacteria; BAB36468; BAB36468; ECs_3045.
DR GeneID; 67414563; -.
DR GeneID; 916749; -.
DR KEGG; ece:Z3409; -.
DR KEGG; ecs:ECs_3045; -.
DR PATRIC; fig|386585.9.peg.3173; -.
DR eggNOG; COG0302; Bacteria.
DR HOGENOM; CLU_049768_3_2_6; -.
DR OMA; CEHMCMS; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..222
FT /note="GTP cyclohydrolase 1"
FT /id="PRO_0000119406"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 222 AA; 24831 MW; 23C6A1440F579FC2 CRC64;
MPSLSKEAAL VHEALVARGL ETPLRPPVHE MDNETRKSLI AGHMTEIMQL LNLDLADDSL
METPHRIAKM YVDEIFSGLD YANFPKITLI ENKMKVDEMV TVRDITLTST CEHHFVTIDG
KATVAYIPKD SVIGLSKINR IVQFFAQRPQ VQERLTQQIL IALQTLLGTN NVAVSIDAVH
YCVKARGIRD ATSATTTTSL GGLFKSSQNT RHEFLRAVRH HN
