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P0A6T5 (GCH1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP cyclohydrolase 1

EC=3.5.4.16
Alternative name(s):
GTP cyclohydrolase I
Short name=GTP-CH-I
Gene names
Name:folE
Ordered Locus Names:b2153, JW2140
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. HAMAP-Rule MF_00223

Enzyme regulation

Allosteric enzyme. Activity is modulated by K+, divalent cations, UTP, and tetrahydrobiopterin. Tetrahydrobiopterin is an inhibitor of this enzyme. HAMAP-Rule MF_00223

Pathway

Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP-Rule MF_00223

Subunit structure

Toroid-shaped homodecamer, composed of two pentamers of five dimers. Ref.8 Ref.11

Sequence similarities

Belongs to the GTP cyclohydrolase I family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.7
Chain2 – 222221GTP cyclohydrolase 1 HAMAP-Rule MF_00223
PRO_0000119404

Sites

Metal binding1111Zinc
Metal binding1141Zinc
Metal binding1821Zinc

Secondary structure

................................... 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6T5 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 23C6A1440F579FC2

FASTA22224,831
        10         20         30         40         50         60 
MPSLSKEAAL VHEALVARGL ETPLRPPVHE MDNETRKSLI AGHMTEIMQL LNLDLADDSL 

        70         80         90        100        110        120 
METPHRIAKM YVDEIFSGLD YANFPKITLI ENKMKVDEMV TVRDITLTST CEHHFVTIDG 

       130        140        150        160        170        180 
KATVAYIPKD SVIGLSKINR IVQFFAQRPQ VQERLTQQIL IALQTLLGTN NVAVSIDAVH 

       190        200        210        220 
YCVKARGIRD ATSATTTTSL GGLFKSSQNT RHEFLRAVRH HN 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"Atomic structure of GTP cyclohydrolase I."
Nar H., Huber R., Meining W., Schmid C., Weinkauf S., Bacher A.
Structure 3:459-466(1995) [PubMed] [Europe PMC] [Abstract]
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]"Zinc plays a key role in human and bacterial GTP cyclohydrolase I."
Auerbach G., Herrmann A., Bracher A., Bader G., Gutlich M., Fischer M., Neukamm M., Garrido-Franco M., Richardson J., Nar H., Huber R., Bacher A.
Proc. Natl. Acad. Sci. U.S.A. 97:13567-13572(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT, ZINC-BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63910 Genomic DNA. Translation: CAA45365.1.
U00007 Genomic DNA. Translation: AAA60535.1.
U00096 Genomic DNA. Translation: AAC75214.1.
AP009048 Genomic DNA. Translation: BAE76630.1.
PIRH64983.
S29895.
RefSeqNP_416658.1. NC_000913.3.
YP_490392.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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/O2-221[»]
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[»]
ProteinModelPortalP0A6T5.
SMRP0A6T5. Positions 2-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid853284. 1 interaction.
DIPDIP-9676N.
IntActP0A6T5. 1 interaction.
MINTMINT-6732927.
STRING511145.b2153.

Proteomic databases

PaxDbP0A6T5.
PRIDEP0A6T5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75214; AAC75214; b2153.
BAE76630; BAE76630; BAE76630.
GeneID12934530.
949040.
KEGGecj:Y75_p2115.
eco:b2153.
PATRIC32119653. VBIEscCol129921_2237.

Organism-specific databases

EchoBASEEB1349.
EcoGeneEG11375. folE.

Phylogenomic databases

eggNOGCOG0302.
HOGENOMHOG000221222.
KOK01495.
OMAVQFFSQR.
OrthoDBEOG6XHC8G.
PhylomeDBP0A6T5.
ProtClustDBPRK09347.

Enzyme and pathway databases

BioCycEcoCyc:GTP-CYCLOHYDRO-I-MONOMER.
ECOL316407:JW2140-MONOMER.
MetaCyc:GTP-CYCLOHYDRO-I-MONOMER.
UniPathwayUPA00848; UER00151.

Gene expression databases

GenevestigatorP0A6T5.

Family and domain databases

HAMAPMF_00223. FolE.
InterProIPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view]
PANTHERPTHR11109. PTHR11109. 1 hit.
PfamPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
TIGRFAMsTIGR00063. folE. 1 hit.
PROSITEPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A6T5.
PROP0A6T5.

Entry information

Entry nameGCH1_ECOLI
AccessionPrimary (citable) accession number: P0A6T5
Secondary accession number(s): P27511, Q2MAS6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene