GTP cyclohydrolase 1 - Escherichia coli (strain K12)

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P0A6T5 (GCH1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 79. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	222 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	GTP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	7,8-dihydroneopterin 3'-triphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway one-carbon metabolic process Inferred from electronic annotation. Source: HAMAP queuosine biosynthetic process Inferred from mutant phenotype PubMed 18931107. Source: EcoCyc tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from direct assay PubMed 4296838 PubMed 821948. Source: EcoliWiki protein complex Inferred from direct assay Ref.9 PubMed 821948. Source: EcoliWiki
Molecular_function	GTP binding Inferred from direct assay PubMed 821948. Source: EcoliWiki GTP cyclohydrolase I activity Inferred from direct assay PubMed 8618856. Source: EcoCyc zinc ion binding Inferred from direct assay Ref.11. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6 Ref.7

Chain

2 – 222

221

GTP cyclohydrolase 1 HAMAP-Rule MF_00223

PRO_0000119404

Sites

Metal binding

111

Zinc

Metal binding

114

Zinc

Metal binding

182

Zinc

Secondary structure

222

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6T5 [UniParc].

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

FASTA

222

24,831

        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' referencesShow '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 277:1453-1474(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.

PIR

H64983.
S29895.

RefSeq

NP_416658.1. NC_000913.2.
YP_490392.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A8R	X-ray	2.10	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O	2-222	[»]
1A9C	X-ray	2.90	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O	2-221	[»]
1FBX	X-ray	2.80	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O	2-222	[»]
1GTP	X-ray	3.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T	2-222	[»]
1N3R	X-ray	2.80	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O	2-222	[»]
1N3S	X-ray	2.55	A/B/C/D/E/F/G/H/I/J	2-222	[»]
1N3T	X-ray	3.20	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O	2-222	[»]

ProteinModelPortal

P0A6T5.

SMR

P0A6T5. Positions 2-222.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-6732927.

STRING

511145.b2153.

Proteomic databases

PaxDb

P0A6T5.

PRIDE

P0A6T5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75214; AAC75214; b2153.
BAE76630; BAE76630; BAE76630.

GeneID

12934530.
949040.

KEGG

ecj:Y75_p2115.
eco:b2153.

PATRIC

32119653. VBIEscCol129921_2237.

Organism-specific databases

EchoBASE

EB1349.

EcoGene

EG11375. folE.

Phylogenomic databases

eggNOG

COG0302.

HOGENOM

HOG000221222.

K01495.

OMA

PTRIAKM.

ProtClustDB

PRK09347.

Enzyme and pathway databases

BioCyc

EcoCyc:GTP-CYCLOHYDRO-I-MONOMER.
ECOL316407:JW2140-MONOMER.
MetaCyc:GTP-CYCLOHYDRO-I-MONOMER.

UniPathway

UPA00848; UER00151.

Gene expression databases

Genevestigator

P0A6T5.

Family and domain databases

HAMAP

MF_00223. FolE.

InterPro

IPR001474. GTP_CycHdrlase_I.
IPR020602. GTP_CycHdrlase_I/CN_OxRdtase.
IPR018234. GTP_CycHdrlase_I_CS.
[Graphical view]

PANTHER

PTHR11109. PTHR11109. 1 hit.

Pfam

PF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00063. folE. 1 hit.

PROSITE

PS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A6T5.

Entry information

Entry name

GCH1_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents