Identification
Name:Riboflavin biosynthesis protein ribF
Synonyms:
  • Riboflavin kinase
  • Flavokinase
  • FMN adenylyltransferase
  • FAD pyrophosphorylase
  • FAD synthase
Gene Name:ribF
Enzyme Class:
Biological Properties
General Function:Involved in FMN adenylyltransferase activity
Specific Function:ATP + riboflavin = ADP + FMN
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0Riboflavin+1.0Thumb+1.0Thumb1.0Adenosine diphosphate+1.0Thumb+1.0Thumb+1.0Thumb
1.0Riboflavin + 1.0Adenosine triphosphate + 1.0Riboflavin → 1.0Adenosine diphosphate + 1.0Hydrogen ion + 1.0Flavin Mononucleotide + 1.0ADP
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb1.0Pyrophosphate+1.0Thumb
EcoCyc Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01248FADMetaboCard
ECMDB01520Flavin MononucleotideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB00244RiboflavinMetaboCard
GO Classification:
Function
adenylyltransferase activity
catalytic activity
FMN adenylyltransferase activity
kinase activity
nucleotidyltransferase activity
riboflavin kinase activity
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
metabolic process
nitrogen compound metabolic process
riboflavin biosynthetic process
riboflavin metabolic process
Gene Properties
Blattner:b0025
Gene OrientationClockwise
Centisome Percentage:0.46
Left Sequence End21407
Right Sequence End22348
Gene Sequence:
>942 bp
ATGAAGCTGATACGCGGCATACATAATCTCAGCCAGGCCCCGCAAGAAGGGTGTGTGCTG
ACTATTGGTAATTTCGACGGCGTGCATCGCGGTCATCGCGCGCTGTTACAGGGCTTGCAG
GAAGAAGGGCGCAAGCGCAACTTACCGGTGATGGTGATGCTTTTTGAACCTCAACCACTG
GAACTGTTTGCTACCGATAAAGCCCCGGCAAGACTGACCCGGCTGCGGGAAAAACTGCGT
TACCTTGCAGAGTGTGGCGTTGATTACGTGCTGTGCGTGCGTTTCGACAGGCGTTTCGCG
GCGTTAACCGCGCAAAATTTCATCAGCGATCTTCTGGTGAAGCATTTGCGCGTAAAATTT
CTTGCCGTAGGTGATGATTTCCGCTTTGGCGCTGGTCGTGAAGGCGATTTCTTGTTATTA
CAGAAAGCTGGCATGGAATACGGCTTCGATATCACCAGTACGCAAACTTTTTGCGAAGGT
GGCGTGCGCATCAGCAGCACCGCCGTGCGTCAGGCCCTTGCGGATGACAATCTGGCTCTG
GCAGAGAGTTTACTGGGGCACCCGTTTGCCATCTCCGGGCGTGTAGTCCACGGTGATGAA
TTAGGGCGCACTATAGGTTTCCCGACGGCGAATGTACCGCTGCGCCGTCAGGTTTCCCCG
GTGAAAGGGGTTTATGCGGTAGAAGTGCTGGGCCTCGGTGAAAAGCCGTTACCCGGCGTG
GCAAACATCGGAACACGCCCAACGGTTGCCGGTATTCGCCAGCAGCTGGAAGTGCATTTG
TTAGATGTTGCAATGGACCTTTACGGTCGCCATATACAAGTAGTGCTGCGTAAAAAAATA
CGCAATGAGCAGCGATTTGCGTCGCTGGACGAACTGAAAGCGCAGATTGCGCGTGATGAA
TTAACCGCCCGCGAATTTTTTGGGCTAACAAAACCGGCTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:313
Protein Molecular Weight:34734
Protein Theoretical pI:10
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Riboflavin biosynthesis protein ribF
MKLIRGIHNLSQAPQEGCVLTIGNFDGVHRGHRALLQGLQEEGRKRNLPVMVMLFEPQPL
ELFATDKAPARLTRLREKLRYLAECGVDYVLCVRFDRRFAALTAQNFISDLLVKHLRVKF
LAVGDDFRFGAGREGDFLLLQKAGMEYGFDITSTQTFCEGGVRISSTAVRQALADDNLAL
AESLLGHPFAISGRVVHGDELGRTIGFPTANVPLRRQVSPVKGVYAVEVLGLGEKPLPGV
ANIGTRPTVAGIRQQLEVHLLDVAMDLYGRHIQVVLRKKIRNEQRFASLDELKAQIARDE
LTAREFFGLTKPA
References
External Links:
ResourceLink
Uniprot ID:P0AG40
Uniprot Name:RIBF_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674289
Ecogene ID:EG11079
Ecocyc:EG11079
ColiBase:b0025
Kegg Gene:b0025
EchoBASE ID:EB1071
CCDB:RIBF_ECOLI
BacMap:16128019
General Reference:
  • 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
  • Kamio, Y., Lin, C. K., Regue, M., Wu, H. C. (1985). "Characterization of the ileS-lsp operon in Escherichia coli. Identification of an open reading frame upstream of the ileS gene and potential promoter(s) for the ileS-lsp operon." J Biol Chem 260:5616-5620. Pubmed: 2985604
  • Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901