ID   GCH1_ECOLI              Reviewed;         222 AA.
AC   P0A6T5; P27511; Q2MAS6;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 146.
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=b2153, JW2140;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=K12;
RX   PubMed=1665332; DOI=10.1515/bchm3.1991.372.2.991;
RA   Katzenmeier G., Schmid C., Kellermann J., Lottspeich F., Bacher A.;
RT   "Biosynthesis of tetrahydrofolate. Sequence of GTP cyclohydrolase I from
RT   Escherichia coli.";
RL   Biol. Chem. Hoppe-Seyler 372:991-997(1991).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=8304099; DOI=10.1007/978-1-4615-2960-6_30;
RA   Schmid C., Meining W., Weinkauf S., Bachmann L., Ritz H., Eberhardt S.,
RA   Gimbel W., Werner T., Lahm H.W., Nar H., Bacher A.;
RT   "Studies on GTP cyclohydrolase I of Escherichia coli.";
RL   Adv. Exp. Med. Biol. 338:157-162(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / BHB2600;
RA   Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA   Church G.M.;
RT   "Automated multiplex sequencing of the E.coli genome.";
RL   Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-51 AND 99-129, AND CHARACTERIZATION.
RX   PubMed=1459137; DOI=10.1111/j.1432-1033.1992.tb17455.x;
RA   Schoedon G., Redweik U., Frank G., Cotton R.G.H., Blau N.;
RT   "Allosteric characteristics of GTP cyclohydrolase I from Escherichia
RT   coli.";
RL   Eur. J. Biochem. 210:561-568(1992).
RN   [7]
RP   PROTEIN SEQUENCE OF 2-13.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded in the
RT   genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [8]
RP   SUBUNIT.
RX   PubMed=12297008; DOI=10.5483/bmbrep.2002.35.3.255;
RA   Lee S., Ahn C., Park E., Hwang D.S., Yim J.;
RT   "Biochemical characterization of oligomerization of Escherichia coli GTP
RT   cyclohydrolase I.";
RL   J. Biochem. Mol. Biol. 35:255-261(2002).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=7663943; DOI=10.1016/s0969-2126(01)00179-4;
RA   Nar H., Huber R., Meining W., Schmid C., Weinkauf S., Bacher A.;
RT   "Atomic structure of GTP cyclohydrolase I.";
RL   Structure 3:459-466(1995).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT SER-113.
RX   PubMed=12559918; DOI=10.1016/s0022-2836(02)01303-7;
RA   Rebelo J., Auerbach G., Bader G., Bracher A., Nar H., Hosl C., Schramek N.,
RA   Kaiser J., Bacher A., Huber R., Fischer M.;
RT   "Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I.";
RL   J. Mol. Biol. 326:503-516(2003).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT, AND ZINC-BINDING SITES.
RX   PubMed=11087827; DOI=10.1073/pnas.240463497;
RA   Auerbach G., Herrmann A., Bracher A., Bader G., Gutlich M., Fischer M.,
RA   Neukamm M., Garrido-Franco M., Richardson J., Nar H., Huber R., Bacher A.;
RT   "Zinc plays a key role in human and bacterial GTP cyclohydrolase I.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:13567-13572(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   -!- ACTIVITY REGULATION: Allosteric enzyme. Activity is modulated by K(+),
CC       divalent cations, UTP, and tetrahydrobiopterin. Tetrahydrobiopterin is
CC       an inhibitor of this enzyme.
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:0000269|PubMed:11087827, ECO:0000269|PubMed:12297008}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. {ECO:0000305}.
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DR   EMBL; X63910; CAA45365.1; -; Genomic_DNA.
DR   EMBL; U00007; AAA60535.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75214.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76630.1; -; Genomic_DNA.
DR   PIR; H64983; H64983.
DR   PIR; S29895; S29895.
DR   RefSeq; NP_416658.1; NC_000913.3.
DR   RefSeq; WP_001139613.1; NZ_STEB01000002.1.
DR   PDB; 1A8R; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=2-222.
DR   PDB; 1A9C; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=2-222.
DR   PDB; 1FBX; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=2-222.
DR   PDB; 1GTP; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=2-222.
DR   PDB; 1N3R; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=2-222.
DR   PDB; 1N3S; X-ray; 2.55 A; A/B/C/D/E/F/G/H/I/J=2-222.
DR   PDB; 1N3T; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=2-222.
DR   PDBsum; 1A8R; -.
DR   PDBsum; 1A9C; -.
DR   PDBsum; 1FBX; -.
DR   PDBsum; 1GTP; -.
DR   PDBsum; 1N3R; -.
DR   PDBsum; 1N3S; -.
DR   PDBsum; 1N3T; -.
DR   AlphaFoldDB; P0A6T5; -.
DR   SMR; P0A6T5; -.
DR   BioGRID; 4263524; 298.
DR   BioGRID; 853284; 1.
DR   DIP; DIP-9676N; -.
DR   IntAct; P0A6T5; 1.
DR   MINT; P0A6T5; -.
DR   STRING; 511145.b2153; -.
DR   jPOST; P0A6T5; -.
DR   PaxDb; 511145-b2153; -.
DR   EnsemblBacteria; AAC75214; AAC75214; b2153.
DR   GeneID; 83580246; -.
DR   GeneID; 949040; -.
DR   KEGG; ecj:JW2140; -.
DR   KEGG; eco:b2153; -.
DR   PATRIC; fig|1411691.4.peg.88; -.
DR   EchoBASE; EB1349; -.
DR   eggNOG; COG0302; Bacteria.
DR   HOGENOM; CLU_049768_3_2_6; -.
DR   InParanoid; P0A6T5; -.
DR   OMA; CEHMCMS; -.
DR   OrthoDB; 9801207at2; -.
DR   PhylomeDB; P0A6T5; -.
DR   BioCyc; EcoCyc:GTP-CYCLOHYDRO-I-MONOMER; -.
DR   BioCyc; MetaCyc:GTP-CYCLOHYDRO-I-MONOMER; -.
DR   BRENDA; 3.5.4.16; 2026.
DR   UniPathway; UPA00848; UER00151.
DR   EvolutionaryTrace; P0A6T5; -.
DR   PRO; PR:P0A6T5; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0032991; C:protein-containing complex; IDA:EcoliWiki.
DR   GO; GO:0005525; F:GTP binding; IDA:EcoliWiki.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
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:0008616; P:queuosine biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00642; GTP_cyclohydro1; 1.
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   NCBIfam; TIGR00063; folE; 1.
DR   PANTHER; PTHR11109:SF7; GTP CYCLOHYDROLASE 1; 1.
DR   PANTHER; PTHR11109; GTP CYCLOHYDROLASE I; 1.
DR   Pfam; PF01227; GTP_cyclohydroI; 1.
DR   SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
DR   PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
DR   PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; Direct protein sequencing; GTP-binding;
KW   Hydrolase; Metal-binding; Nucleotide-binding; One-carbon metabolism;
KW   Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1459137,
FT                   ECO:0000269|PubMed:9298646"
FT   CHAIN           2..222
FT                   /note="GTP cyclohydrolase 1"
FT                   /id="PRO_0000119404"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   HELIX           6..17
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   HELIX           33..50
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   HELIX           58..61
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   HELIX           63..73
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   TURN            74..76
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   HELIX           81..83
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   STRAND          100..111
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   TURN            112..115
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   STRAND          116..126
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   STRAND          129..133
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   HELIX           135..146
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   STRAND          147..150
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   HELIX           152..167
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   STRAND          172..180
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   HELIX           181..184
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   STRAND          194..200
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   HELIX           203..206
FT                   /evidence="ECO:0007829|PDB:1A8R"
FT   HELIX           208..217
FT                   /evidence="ECO:0007829|PDB:1A8R"
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
//