Riboflavin synthase alpha chain (P0AFU8)

Identification
Name:Riboflavin synthase alpha chain
Synonyms:Not Available
Gene Name:ribE
Enzyme Class:
Biological Properties
General Function:Involved in riboflavin synthase activity
Specific Function:Riboflavin synthase is a bifunctional enzyme complex catalyzing the formation of riboflavin from 5-amino-6-(1'-D)- ribityl-amino-2,4(1H,3H)-pyrimidinedione and L-3,4-dihydrohy-2- butanone-4-phosphate via 6,7-dimethyl-8-lumazine. The alpha subunit catalyzes the dismutation of 6,7-dimethyl-8-lumazine to riboflavin and 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)- pyrimidinedione
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
2.0Thumb → 1.0Thumb+1.0Thumb
2.06,7-Dimethyl-8-(1-D-ribityl)lumazine → 1.05-Amino-6-ribitylamino uracil + 1.0Riboflavin
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+2.0Thumb+1.0Thumb
1.05-Amino-6-ribitylamino uracil + 1.03,4-Dihydroxy-2-butanone-4-P → 1.06,7-Dimethyl-8-(1-D-ribityl)lumazine + 2.0Water + 1.0Phosphate
ReactionCard
2.0Thumb ↔ 1.0Thumb+1.0Thumb
2.06,7-Dimethyl-8-(1-D-ribityl)lumazine ↔ 1.0Riboflavin + 1.05-Amino-6-ribitylamino uracil
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.06,7-Dimethyl-8-(1-D-ribityl)lumazine+1.0Thumb
1.05-Amino-6-ribitylamino uracil + 1.01-Deoxy-L-glycero-tetrulose 4-phosphate → 1.0Water + 1.0Phosphate + 1.0Hydrogen ion + 1.06,7-Dimethyl-8-(1-D-ribityl)lumazine + 1.06,7-Dimethyl-8-(1-D-ribityl)lumazine
ReactionCard
1.06,7-Dimethyl-8-(1-D-ribityl)lumazine+1.0Thumb+1.0Thumb → 1.0Riboflavin+1.0Thumb+1.0Thumb
1.06,7-Dimethyl-8-(1-D-ribityl)lumazine + 1.0Hydrogen ion + 1.06,7-Dimethyl-8-(1-D-ribityl)lumazine → 1.0Riboflavin + 1.05-Amino-6-ribitylamino uracil + 1.0Riboflavin
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Adenosine + 1.0Water → 1.0beta-D-ribofuranose + 1.0Adenine
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB231221-Deoxy-L-glycero-tetrulose 4-phosphateMetaboCard
ECMDB040603,4-Dihydroxy-2-butanone-4-PMetaboCard
ECMDB230165-amino-6-(D-ribitylamino)uracilMetaboCard
ECMDB041455-Amino-6-ribitylamino uracilMetaboCard
ECMDB038266,7-Dimethyl-8-(1-D-ribityl)lumazineMetaboCard
ECMDB00034AdenineMetaboCard
ECMDB00050AdenosineMetaboCard
ECMDB20343beta-D-ribofuranoseMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00244RiboflavinMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
riboflavin synthase activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
metabolic process
nitrogen compound metabolic process
riboflavin biosynthetic process
riboflavin metabolic process
Gene Properties
Blattner:b1662
Gene OrientationCounterclockwise
Centisome Percentage:37.52
Left Sequence End1740625
Right Sequence End1741266
Gene Sequence:
>642 bp
ATGCGCAGTAAGTATATCGTCATTGAGGGGCTGGAAGGCGCAGGCAAAACTACCGCGCGT
AATGTGGTGGTTGAGACGCTCGAGCAACTGGGTATCCGCGACATGGTTTTCACTCGGGAA
CCTGGCGGTACGCAACTTGCCGAAAAGTTAAGAAGCCTGGTGCTGGATATCAAATCGGTA
GGCGATGAAGTCATTACCGATAAAGCCGAAGTTCTGATGTTTTATGCCGCGCGCGTTCAA
CTGGTAGAAACGGTCATCAAACCAGCTCTGGCTAACGGCACCTGGGTGATTGGCGATCGC
CACGATCTCTCCACTCAGGCGTATCAGGGCGGCGGACGTGGTATTGACCAACATATGCTG
GCAACACTGCGTGATGCTGTTCTCGGGGATTTTCGCCCCGACTTAACGCTCTATCTCGAT
GTTACCCCGGAAGTTGGCTTAAAACGCGCGCGTGCGCGCGGCGAGCTGGATCGTATTGAG
CAAGAATCTTTCGATTTCTTTAATCGCACCCGCGCCCGCTATCTGGAACTGGCAGCACAA
GATAAAAGCATTCATACCATTGATGCCACCCAGCCGCTGGAGGCCGTGATGGATGCAATC
CGCACTACCGTGACCCACTGGGTGAAGGAGTTGGACGCATGA
Protein Properties
Pfam Domain Function:
Protein Residues:213
Protein Molecular Weight:23445
Protein Theoretical pI:6
PDB File:1I8D
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Riboflavin synthase alpha chain
MFTGIVQGTAKLVSIDEKPNFRTHVVELPDHMLDGLETGASVAHNGCCLTVTEINGNHVS
FDLMKETLRITNLGDLKVGDWVNVERAAKFSDEIGGHLMSGHIMTTAEVAKILTSENNRQ
IWFKVQDSQLMKYILYKGFIGIDGISLTVGEVTPTRFCVHLIPETLERTTLGKKKLGARV
NIEIDPQTQAVVDTVERVLAARENAMNQPGTEA
References
External Links:
ResourceLink
Uniprot ID:P0AFU8
Uniprot Name:RISA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062665
PDB ID:1I8D
Ecogene ID:EG11406
Ecocyc:EG11406
ColiBase:b1662
Kegg Gene:b1662
EchoBASE ID:EB1298
CCDB:RISA_ECOLI
BacMap:16129620
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
  • Eberhardt, S., Richter, G., Gimbel, W., Werner, T., Bacher, A. (1996). "Cloning, sequencing, mapping and hyperexpression of the ribC gene coding for riboflavin synthase of Escherichia coli." Eur J Biochem 242:712-719. Pubmed: 9022701
  • 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
  • Hensel, M., Shea, J. E., Baumler, A. J., Gleeson, C., Blattner, F., Holden, D. W. (1997). "Analysis of the boundaries of Salmonella pathogenicity island 2 and the corresponding chromosomal region of Escherichia coli K-12." J Bacteriol 179:1105-1111. Pubmed: 9023191
  • Liao, D. I., Wawrzak, Z., Calabrese, J. C., Viitanen, P. V., Jordan, D. B. (2001). "Crystal structure of riboflavin synthase." Structure 9:399-408. Pubmed: 11377200
  • Truffault, V., Coles, M., Diercks, T., Abelmann, K., Eberhardt, S., Luttgen, H., Bacher, A., Kessler, H. (2001). "The solution structure of the N-terminal domain of riboflavin synthase." J Mol Biol 309:949-960. Pubmed: 11399071