GTP cyclohydrolase-2 (P0A7I7)

Identification
Name:GTP cyclohydrolase-2
Synonyms:
  • GTP cyclohydrolase II
Gene Name:ribA
Enzyme Class:
Biological Properties
General Function:Involved in GTP cyclohydrolase II activity
Specific Function:Catalyzes the conversion of GTP to 2,5-diamino-6- ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate
Cellular Location:Cytoplasmic
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Thumb+3.0Thumb ↔ 1.0Thumb+1.0Thumb+2.0Thumb+1.0Thumb+1.0Thumb
1.0Guanosine triphosphate + 3.0Water ↔ 1.02,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + 1.0Formic acid + 2.0Hydrogen ion + 1.0Pyrophosphate + 1.02,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine
ReactionCard
1.0Thumb+3.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Guanosine triphosphate + 3.0Water ↔ 1.0Formic acid + 1.02,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + 1.0Pyrophosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+3.0Thumb ↔ 1.0Thumb+1.0Thumb+2.0Thumb+1.0Thumb+1.0Thumb
1.0Guanosine triphosphate + 3.0Water ↔ 1.02,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + 1.0Formic acid + 2.0Hydrogen ion + 1.0Pyrophosphate + 1.02,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine
ReactionCard
Complex Reactions:
1.0Thumb+3.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Guanosine triphosphate + 3.0Water → 1.0Formic acid + 1.02,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + 1.0Pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB040522,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidineMetaboCard
ECMDB00142Formic acidMetaboCard
ECMDB01273Guanosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
cyclohydrolase activity
GTP cyclohydrolase activity
GTP cyclohydrolase II 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
metabolic process
nitrogen compound metabolic process
riboflavin biosynthetic process
riboflavin metabolic process
Gene Properties
Blattner:b1277
Gene OrientationCounterclockwise
Centisome Percentage:28.81
Left Sequence End1336594
Right Sequence End1337184
Gene Sequence:
>591 bp
ATGCAGTCTGAACGTATTTATTTGGTATGGGCCCATCCTCGTCATGATTCATTGACCGCA
CATATTGCTGATGCGATCCATCAGCGGGCAATGGAGCGGAAAATACAGGTGACGGAACTC
GATTTATATCGGCGTAATTTCAACCCAGTGATGACGCCGGAAGATGAACCAGACTGGAAG
AATATGGATAAACGTTATTCTCCAGAGGTTCATCAGCTTTATTCAGAGCTGCTTGAACAT
GACACGTTAGTGGTGGTTTTTCCTCTCTGGTGGTACAGCTTCCCGGCAATGCTAAAAGGA
TATATTGACAGAGTATGGAATAATGGGCTGGCTTATGGAGATGGGCACAAATTACCATTC
AATAAAGTTCGTTGGGTGGCGCTGGTTGGAGGAGACAAAGAATCATTTGTCCAGATGGGC
TGGGAAAAAAATATAAGCGATTATTTAAAAAATATGTGCAGTTATCTTGGTATTGAAGAT
GCCGATGTCACTTTCTTGTGTAATACAGTGGTATTCGATGGGGAAGAACTTCACGCGAGC
TATTATCAGTCGTTATTATCTCAGGTACGGGATATGGTAGATGCACTATAA
Protein Properties
Pfam Domain Function:
Protein Residues:196
Protein Molecular Weight:21836
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>GTP cyclohydrolase-2
MQLKRVAEAKLPTPWGDFLMVGFEELATGHDHVALVYGDISGHTPVLARVHSECLTGDAL
FSLRCDCGFQLEAALTQIAEEGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQ
LGFAADERDFTLCADMFKLLGVNEVRLLTNNPKKVEILTEAGINIVERVPLIVGRNPNNE
HYLDTKAEKMGHLLNK
References
External Links:
ResourceLink
Uniprot ID:P0A7I7
Uniprot Name:RIBA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062477
Ecogene ID:EG11331
Ecocyc:EG11331
ColiBase:b1277
Kegg Gene:b1277
EchoBASE ID:EB1307
CCDB:RIBA_ECOLI
BacMap:16129238
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • 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
  • Foor, F., Brown, G. M. (1975). "Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli." J Biol Chem 250:3545-3551. Pubmed: 235552
  • 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
  • Kaiser, J., Schramek, N., Eberhardt, S., Puttmer, S., Schuster, M., Bacher, A. (2002). "Biosynthesis of vitamin B2." Eur J Biochem 269:5264-5270. Pubmed: 12392559
  • Prodromou, C., Artymiuk, P. J., Guest, J. R. (1992). "The aconitase of Escherichia coli. Nucleotide sequence of the aconitase gene and amino acid sequence similarity with mitochondrial aconitases, the iron-responsive-element-binding protein and isopropylmalate isomerases." Eur J Biochem 204:599-609. Pubmed: 1541275
  • Ren, J., Kotaka, M., Lockyer, M., Lamb, H. K., Hawkins, A. R., Stammers, D. K. (2005). "GTP cyclohydrolase II structure and mechanism." J Biol Chem 280:36912-36919. Pubmed: 16115872
  • Richter, G., Ritz, H., Katzenmeier, G., Volk, R., Kohnle, A., Lottspeich, F., Allendorf, D., Bacher, A. (1993). "Biosynthesis of riboflavin: cloning, sequencing, mapping, and expression of the gene coding for GTP cyclohydrolase II in Escherichia coli." J Bacteriol 175:4045-4051. Pubmed: 8320220
  • Ritz, H., Schramek, N., Bracher, A., Herz, S., Eisenreich, W., Richter, G., Bacher, A. (2001). "Biosynthesis of riboflavin: studies on the mechanism of GTP cyclohydrolase II." J Biol Chem 276:22273-22277. Pubmed: 11301327