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P0A6T5

- GCH1_ECOLI

UniProt

P0A6T5 - GCH1_ECOLI

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Protein

GTP cyclohydrolase 1

Gene
folE, b2153, JW2140
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.UniRule annotation

Enzyme regulationi

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

Pathwayi

Sites

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

GO - Molecular functioni

  1. GTP binding Source: EcoliWiki
  2. GTP cyclohydrolase I activity Source: EcoCyc
  3. zinc ion binding Source: EcoCyc

GO - Biological processi

  1. 7,8-dihydroneopterin 3'-triphosphate biosynthetic process Source: UniProtKB-UniPathway
  2. one-carbon metabolic process Source: UniProtKB-HAMAP
  3. queuosine biosynthetic process Source: EcoCyc
  4. tetrahydrofolate biosynthetic process Source: UniProtKB-HAMAP
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.
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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11375. folE.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
  2. protein complex Source: EcoliWiki
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 222221GTP cyclohydrolase 1UniRule annotationPRO_0000119404Add
BLAST

Proteomic databases

PaxDbiP0A6T5.
PRIDEiP0A6T5.

Expressioni

Gene expression databases

GenevestigatoriP0A6T5.

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 – 1712
Helixi33 – 5018
Helixi58 – 614
Helixi63 – 7311
Turni74 – 763
Helixi77 – 793
Helixi81 – 833
Beta strandi89 – 913
Beta strandi100 – 11112
Turni112 – 1154
Beta strandi116 – 12611
Beta strandi129 – 1335
Helixi135 – 14612
Beta strandi147 – 1504
Helixi152 – 16716
Beta strandi172 – 1809
Helixi181 – 1844
Beta strandi194 – 2007
Helixi203 – 2064
Helixi208 – 21710

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP0A6T5.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0302.
HOGENOMiHOG000221222.
KOiK01495.
OMAiQRIAEHM.
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

MPSLSKEAAL VHEALVARGL ETPLRPPVHE MDNETRKSLI AGHMTEIMQL    50
LNLDLADDSL METPHRIAKM YVDEIFSGLD YANFPKITLI ENKMKVDEMV 100
TVRDITLTST CEHHFVTIDG KATVAYIPKD SVIGLSKINR IVQFFAQRPQ 150
VQERLTQQIL IALQTLLGTN NVAVSIDAVH YCVKARGIRD ATSATTTTSL 200
GGLFKSSQNT RHEFLRAVRH HN 222
Length:222
Mass (Da):24,831
Last modified:January 23, 2007 - v2
Checksum:i23C6A1440F579FC2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_490392.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75214; AAC75214; b2153.
BAE76630; BAE76630; BAE76630.
GeneIDi12934530.
949040.
KEGGiecj:Y75_p2115.
eco:b2153.
PATRICi32119653. VBIEscCol129921_2237.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi H64983.
S29895.
RefSeqi NP_416658.1. NC_000913.3.
YP_490392.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 2-222 [» ]
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 [» ]
ProteinModelPortali P0A6T5.
SMRi P0A6T5. Positions 2-222.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 853284. 1 interaction.
DIPi DIP-9676N.
IntActi P0A6T5. 1 interaction.
MINTi MINT-6732927.
STRINGi 511145.b2153.

Proteomic databases

PaxDbi P0A6T5.
PRIDEi P0A6T5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75214 ; AAC75214 ; b2153 .
BAE76630 ; BAE76630 ; BAE76630 .
GeneIDi 12934530.
949040.
KEGGi ecj:Y75_p2115.
eco:b2153.
PATRICi 32119653. VBIEscCol129921_2237.

Organism-specific databases

EchoBASEi EB1349.
EcoGenei EG11375. folE.

Phylogenomic databases

eggNOGi COG0302.
HOGENOMi HOG000221222.
KOi K01495.
OMAi QRIAEHM.
OrthoDBi EOG6XHC8G.
PhylomeDBi P0A6T5.

Enzyme and pathway databases

UniPathwayi UPA00848 ; UER00151 .
BioCyci EcoCyc:GTP-CYCLOHYDRO-I-MONOMER.
ECOL316407:JW2140-MONOMER.
MetaCyc:GTP-CYCLOHYDRO-I-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A6T5.
PROi P0A6T5.

Gene expression databases

Genevestigatori P0A6T5.

Family and domain databases

HAMAPi MF_00223. FolE.
InterProi IPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view ]
PANTHERi PTHR11109. PTHR11109. 1 hit.
Pfami PF01227. GTP_cyclohydroI. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00063. folE. 1 hit.
PROSITEi PS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 9, 2014
This is version 88 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

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