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Protein

GTP cyclohydrolase 1

Gene

folE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.

Enzyme regulationi

Allosteric enzyme. Activity is modulated by K+, divalent cations, UTP, and tetrahydrobiopterin. Tetrahydrobiopterin is an inhibitor of this enzyme.

Pathway:i7,8-dihydroneopterin triphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 7,8-dihydroneopterin triphosphate from GTP.
Proteins known to be involved in this subpathway in this organism are:
  1. GTP cyclohydrolase 1 (folE)
This subpathway is part of the pathway 7,8-dihydroneopterin triphosphate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 7,8-dihydroneopterin triphosphate from GTP, the pathway 7,8-dihydroneopterin triphosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi111 – 1111Zinc
Metal bindingi114 – 1141Zinc
Metal bindingi182 – 1821Zinc

GO - Molecular functioni

  • GTP binding Source: EcoliWiki
  • GTP cyclohydrolase I activity Source: EcoCyc
  • zinc ion binding Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

GTP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:GTP-CYCLOHYDRO-I-MONOMER.
ECOL316407:JW2140-MONOMER.
MetaCyc:GTP-CYCLOHYDRO-I-MONOMER.
BRENDAi3.5.4.16. 2026.
UniPathwayiUPA00848; UER00151.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase 1 (EC:3.5.4.16)
Alternative name(s):
GTP cyclohydrolase I
Short name:
GTP-CH-I
Gene namesi
Name:folE
Ordered Locus Names:b2153, JW2140
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11375. folE.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • protein complex Source: EcoliWiki
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 222221GTP cyclohydrolase 1PRO_0000119404Add
BLAST

Proteomic databases

PaxDbiP0A6T5.
PRIDEiP0A6T5.

Interactioni

Subunit structurei

Toroid-shaped homodecamer, composed of two pentamers of five dimers.2 Publications

Protein-protein interaction databases

BioGridi853284. 1 interaction.
DIPiDIP-9676N.
IntActiP0A6T5. 1 interaction.
MINTiMINT-6732927.
STRINGi511145.b2153.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1712Combined sources
Helixi33 – 5018Combined sources
Helixi58 – 614Combined sources
Helixi63 – 7311Combined sources
Turni74 – 763Combined sources
Helixi77 – 793Combined sources
Helixi81 – 833Combined sources
Beta strandi89 – 913Combined sources
Beta strandi100 – 11112Combined sources
Turni112 – 1154Combined sources
Beta strandi116 – 12611Combined sources
Beta strandi129 – 1335Combined sources
Helixi135 – 14612Combined sources
Beta strandi147 – 1504Combined sources
Helixi152 – 16716Combined sources
Beta strandi172 – 1809Combined sources
Helixi181 – 1844Combined sources
Beta strandi194 – 2007Combined sources
Helixi203 – 2064Combined sources
Helixi208 – 21710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8RX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-222[»]
1A9CX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-222[»]
1FBXX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-222[»]
1GTPX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T2-222[»]
1N3RX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-222[»]
1N3SX-ray2.55A/B/C/D/E/F/G/H/I/J2-222[»]
1N3TX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-222[»]
ProteinModelPortaliP0A6T5.
SMRiP0A6T5. Positions 2-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6T5.

Family & Domainsi

Sequence similaritiesi

Belongs to the GTP cyclohydrolase I family.Curated

Phylogenomic databases

eggNOGiCOG0302.
HOGENOMiHOG000221222.
InParanoidiP0A6T5.
KOiK01495.
OMAiMNRIVEY.
OrthoDBiEOG6XHC8G.
PhylomeDBiP0A6T5.

Family and domain databases

HAMAPiMF_00223. FolE.
InterProiIPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view]
PANTHERiPTHR11109. PTHR11109. 1 hit.
PfamiPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00063. folE. 1 hit.
PROSITEiPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6T5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSLSKEAAL VHEALVARGL ETPLRPPVHE MDNETRKSLI AGHMTEIMQL
60 70 80 90 100
LNLDLADDSL METPHRIAKM YVDEIFSGLD YANFPKITLI ENKMKVDEMV
110 120 130 140 150
TVRDITLTST CEHHFVTIDG KATVAYIPKD SVIGLSKINR IVQFFAQRPQ
160 170 180 190 200
VQERLTQQIL IALQTLLGTN NVAVSIDAVH YCVKARGIRD ATSATTTTSL
210 220
GGLFKSSQNT RHEFLRAVRH HN
Length:222
Mass (Da):24,831
Last modified:January 23, 2007 - v2
Checksum:i23C6A1440F579FC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63910 Genomic DNA. Translation: CAA45365.1.
U00007 Genomic DNA. Translation: AAA60535.1.
U00096 Genomic DNA. Translation: AAC75214.1.
AP009048 Genomic DNA. Translation: BAE76630.1.
PIRiH64983.
S29895.
RefSeqiNP_416658.1. NC_000913.3.
WP_001139613.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC75214; AAC75214; b2153.
BAE76630; BAE76630; BAE76630.
GeneIDi949040.
KEGGieco:b2153.
PATRICi32119653. VBIEscCol129921_2237.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63910 Genomic DNA. Translation: CAA45365.1.
U00007 Genomic DNA. Translation: AAA60535.1.
U00096 Genomic DNA. Translation: AAC75214.1.
AP009048 Genomic DNA. Translation: BAE76630.1.
PIRiH64983.
S29895.
RefSeqiNP_416658.1. NC_000913.3.
WP_001139613.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8RX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-222[»]
1A9CX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-222[»]
1FBXX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-222[»]
1GTPX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T2-222[»]
1N3RX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-222[»]
1N3SX-ray2.55A/B/C/D/E/F/G/H/I/J2-222[»]
1N3TX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-222[»]
ProteinModelPortaliP0A6T5.
SMRiP0A6T5. Positions 2-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi853284. 1 interaction.
DIPiDIP-9676N.
IntActiP0A6T5. 1 interaction.
MINTiMINT-6732927.
STRINGi511145.b2153.

Proteomic databases

PaxDbiP0A6T5.
PRIDEiP0A6T5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75214; AAC75214; b2153.
BAE76630; BAE76630; BAE76630.
GeneIDi949040.
KEGGieco:b2153.
PATRICi32119653. VBIEscCol129921_2237.

Organism-specific databases

EchoBASEiEB1349.
EcoGeneiEG11375. folE.

Phylogenomic databases

eggNOGiCOG0302.
HOGENOMiHOG000221222.
InParanoidiP0A6T5.
KOiK01495.
OMAiMNRIVEY.
OrthoDBiEOG6XHC8G.
PhylomeDBiP0A6T5.

Enzyme and pathway databases

UniPathwayiUPA00848; UER00151.
BioCyciEcoCyc:GTP-CYCLOHYDRO-I-MONOMER.
ECOL316407:JW2140-MONOMER.
MetaCyc:GTP-CYCLOHYDRO-I-MONOMER.
BRENDAi3.5.4.16. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A6T5.
PROiP0A6T5.

Family and domain databases

HAMAPiMF_00223. FolE.
InterProiIPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view]
PANTHERiPTHR11109. PTHR11109. 1 hit.
PfamiPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00063. folE. 1 hit.
PROSITEiPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Biosynthesis of tetrahydrofolate. Sequence of GTP cyclohydrolase I from Escherichia coli."
    Katzenmeier G., Schmid C., Kellermann J., Lottspeich F., Bacher A.
    Biol. Chem. Hoppe-Seyler 372:991-997(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: K12.
  2. "Studies on GTP cyclohydrolase I of Escherichia coli."
    Schmid C., Meining W., Weinkauf S., Bachmann L., Ritz H., Eberhardt S., Gimbel W., Werner T., Lahm H.W., Nar H., Bacher A.
    Adv. Exp. Med. Biol. 338:157-162(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "Automated multiplex sequencing of the E.coli genome."
    Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.
    Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / BHB2600.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Allosteric characteristics of GTP cyclohydrolase I from Escherichia coli."
    Schoedon G., Redweik U., Frank G., Cotton R.G.H., Blau N.
    Eur. J. Biochem. 210:561-568(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-51 AND 99-129, CHARACTERIZATION.
  7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  8. "Biochemical characterization of oligomerization of Escherichia coli GTP cyclohydrolase I."
    Lee S., Ahn C., Park E., Hwang D.S., Yim J.
    J. Biochem. Mol. Biol. 35:255-261(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  10. "Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I."
    Rebelo J., Auerbach G., Bader G., Bracher A., Nar H., Hosl C., Schramek N., Kaiser J., Bacher A., Huber R., Fischer M.
    J. Mol. Biol. 326:503-516(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT SER-113.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT, ZINC-BINDING SITES.

Entry informationi

Entry nameiGCH1_ECOLI
AccessioniPrimary (citable) accession number: P0A6T5
Secondary accession number(s): P27511, Q2MAS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.