ECMDB: GTP cyclohydrolase 1 (P0A6T5)

Identification

Name:

GTP cyclohydrolase 1

Synonyms:

GTP cyclohydrolase I
GTP-CH-I

Gene Name:

folE

Enzyme Class:

3.5.4.16

Biological Properties

General Function:

Involved in GTP cyclohydrolase I activity

Specific Function:

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

Cellular Location:

Cytoplasmic

SMPDB Pathways:

Flavin biosynthesis PW001971
Folate biosynthesis PW000908
GTP degradation PW001888
Tetrahydromonapterin Biosynthesis PW002043
preQ0 metabolism PW001893

KEGG Pathways:

Folate biosynthesis ec00790
Metabolic pathways eco01100

KEGG Reactions:

1.0

↔

1.0

1.0Guanosine triphosphate + 1.0Water ↔ 1.0Formamidopyrimidine nucleoside triphosphate
ReactionCard

1.0

↔

1.0

1.0Dihydroneopterin triphosphate + 1.0Water ↔ 1.02,5-Diamino-6-(5'-triphosphoryl-3',4'-trihydroxy-2'-oxopentyl)-amino-4-oxopyrimidine
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1.0

↔

1.0

1.0Formamidopyrimidine nucleoside triphosphate + 1.0Water ↔ 1.02,5-Diaminopyrimidine nucleoside triphosphate + 1.0Formic acid
ReactionCard

1.0

↔

1.0

1.02,5-Diaminopyrimidine nucleoside triphosphate ↔ 1.02,5-Diamino-6-(5'-triphosphoryl-3',4'-trihydroxy-2'-oxopentyl)-amino-4-oxopyrimidine
ReactionCard

1.0

↔

1.0

1.0Guanosine triphosphate + 1.0Water ↔ 1.0Formic acid + 1.0Dihydroneopterin triphosphate
ReactionCard

SMPDB Reactions:

1.0

→

1.0

1.0Guanosine triphosphate + 1.0Water → 1.0Formic acid + 1.0Hydrogen ion + 1.07,8-dihydroneopterin 3'-triphosphate
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1.0

3.0

→

1.0

1.0Pyrophosphate

2.0

1.0

1.0Guanosine triphosphate + 3.0Water → 1.0Formic acid + 1.0Pyrophosphate + 2.0Hydrogen ion + 1.02,5-Diamino-6-(5'-phosphoribosylamino)-4-pyrimidineone
ReactionCard

1.0

→

1.0

1.0Pyrophosphate

1.0Guanosine triphosphate + 1.0Water → 1.02,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + 1.0Hydrogen ion + 1.0Formic acid + 1.0Pyrophosphate
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EcoCyc Reactions:

1.0

→

1.0

1.0Guanosine triphosphate + 1.0Water → 1.0Dihydroneopterin triphosphate + 1.0Formic acid + 1.0Hydrogen ion
ReactionCard

Complex Reactions:

1.0

→

1.0

1.02-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate

1.0Guanosine triphosphate + 1.0Water → 1.0Formic acid + 1.02-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB20058	2,5-Diamino-6-(5'-phosphoribosylamino)-4-pyrimidineone	MetaboCard
ECMDB06823	2,5-Diamino-6-(5'-triphosphoryl-3',4'-trihydroxy-2'-oxopentyl)-amino-4-oxopyrimidine	MetaboCard
ECMDB04052	2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine	MetaboCard
ECMDB20059	2,5-Diaminopyrimidine nucleoside triphosphate	MetaboCard
ECMDB24245	7,8-dihydroneopterin 3'-triphosphate	MetaboCard
ECMDB01144	Dihydroneopterin triphosphate	MetaboCard
ECMDB20148	Formamidopyrimidine nucleoside triphosphate	MetaboCard
ECMDB00142	Formic acid	MetaboCard
ECMDB01273	Guanosine triphosphate	MetaboCard
ECMDB21225	Hydrogen ion	MetaboCard
ECMDB00494	Water	MetaboCard

GO Classification:

Component
cell part
cytoplasm
intracellular part
Function
catalytic activity
cyclohydrolase activity
GTP cyclohydrolase activity
GTP cyclohydrolase I activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
Process
cellular aromatic compound metabolic process
cellular metabolic process
folic acid and derivative biosynthetic process
folic acid and derivative metabolic process
metabolic process
tetrahydrofolate biosynthetic process

Gene Properties

Blattner:

b2153

Gene Orientation

Counterclockwise

Centisome Percentage:

48.30

Left Sequence End

2241006

Right Sequence End

2241674

Gene Sequence:

>669 bp
ATGCCCGTCAAGGATTTGACGGGCATTACTGCAAAGGACGCGCAAATGTTATCTGTAGTT
AAACCTCTTCAGGAATTTGGTAAGCTCGATAAATGTTTGTCCAGATACGGTACGCGCTTC
GAGTTTAATAATGAAAAGCAAGTTATATTTTCCAGTGATGTCAATAACGAAGATACTTTC
GTTATTTTAGAGGGAGTTATCTCTCTGCGTAGAGAAGAAAACGTACTTATCGGTATTACC
CAGGCTCCTTATATTATGGGGCTGGCTGATGGTTTAATGAAAAACGATATACCATACAAA
TTAATATCAGAAGGAAATTGTACGGGATATCATCTACCAGCCAAACAAACCATTACGCTT
ATTGAACAAAATCAACTCTGGCGAGACGCTTTTTACTGGTTAGCCTGGCAAAATAGAATT
CTGGAATTACGCGACGTGCAGCTCATTGGGCATAATTCCTACGAACAAATCCGCGCAACA
TTATTATCAATGATTGACTGGAATGAAGAATTGCGATCACGTATTGGTGTGATGAATTAT
ATCCATCAACGTACACGCATATCGCGTTCTGTCGTCGCAGAAGTTCTCGCTGCTTTGCGT
AAAGGCGGCTATATCGAAATGAATAAAGGCAAACTGGTCGCTATCAACCGTTTGCCTTCA
GAGTATTAA

Protein Properties

Pfam Domain Function:

GTP_cyclohydroI (PF01227 )

Protein Residues:

222

Protein Molecular Weight:

24830

Protein Theoretical pI:

PDB File:

1GTP

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>GTP cyclohydrolase 1
MPSLSKEAALVHEALVARGLETPLRPPVHEMDNETRKSLIAGHMTEIMQLLNLDLADDSL
METPHRIAKMYVDEIFSGLDYANFPKITLIENKMKVDEMVTVRDITLTSTCEHHFVTIDG
KATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVH
YCVKARGIRDATSATTTTSLGGLFKSSQNTRHEFLRAVRHHN

References

External Links:

Resource	Link
Uniprot ID:	P0A6T5
Uniprot Name:	GCH1_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	85674516
PDB ID:	1GTP
Ecogene ID:	EG11375
Ecocyc:	EG11375
ColiBase:	b2153
Kegg Gene:	b2153
EchoBASE ID:	EB1349
CCDB:	GCH1_ECOLI
BacMap:	16130091

General Reference:

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. (2000). "Zinc plays a key role in human and bacterial GTP cyclohydrolase I." Proc Natl Acad Sci U S A 97:13567-13572. Pubmed: 11087827
Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
Katzenmeier, G., Schmid, C., Kellermann, J., Lottspeich, F., Bacher, A. (1991). "Biosynthesis of tetrahydrofolate. Sequence of GTP cyclohydrolase I from Escherichia coli." Biol Chem Hoppe Seyler 372:991-997. Pubmed: 1665332
Lee, S., Ahn, C., Park, E., Hwang, D. S., Yim, J. (2002). "Biochemical characterization of oligomerization of Escherichia coli GTP cyclohydrolase I." J Biochem Mol Biol 35:255-261. Pubmed: 12297008
Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
Nar, H., Huber, R., Meining, W., Schmid, C., Weinkauf, S., Bacher, A. (1995). "Atomic structure of GTP cyclohydrolase I." Structure 3:459-466. Pubmed: 7663943
Rebelo, J., Auerbach, G., Bader, G., Bracher, A., Nar, H., Hosl, C., Schramek, N., Kaiser, J., Bacher, A., Huber, R., Fischer, M. (2003). "Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I." J Mol Biol 326:503-516. Pubmed: 12559918
Schmid, C., Meining, W., Weinkauf, S., Bachmann, L., Ritz, H., Eberhardt, S., Gimbel, W., Werner, T., Lahm, H. W., Nar, H., et, a. l. .. (1993). "Studies on GTP cyclohydrolase I of Escherichia coli." Adv Exp Med Biol 338:157-162. Pubmed: 8304099
Schoedon, G., Redweik, U., Frank, G., Cotton, R. G., Blau, N. (1992). "Allosteric characteristics of GTP cyclohydrolase I from Escherichia coli." Eur J Biochem 210:561-568. Pubmed: 1459137