GCH1_ECOLI
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 03-AUG-2022, entry version 138.
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; Proteobacteria; 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; P0A6T5; -.
DR PRIDE; P0A6T5; -.
DR EnsemblBacteria; AAC75214; AAC75214; b2153.
DR EnsemblBacteria; BAE76630; BAE76630; BAE76630.
DR GeneID; 67414563; -.
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 PhylomeDB; P0A6T5; -.
DR BioCyc; EcoCyc:GTP-CYCLOHYDRO-I-MON; -.
DR BioCyc; MetaCyc:GTP-CYCLOHYDRO-I-MON; -.
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 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 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
