General Information |
MoonProt ID | 492 |
First appeared in release | 3.0 |
Name(s) | Bifunctional riboflavin kinase/FMN adenylyltransferase
Gene: ribC
Recommended name:
Bifunctional riboflavin kinase/FMN adenylyltransferase
Alternative name(s):
Riboflavin biosynthesis protein RibF
Including the following 2 domains:
Riboflavin kinase (EC:2.7.1.26)
Alternative name(s):
Flavokinase
FMN adenylyltransferase (EC:2.7.7.2)
Alternative name(s):
FAD pyrophosphorylase
FAD synthase |
UniProt ID | P54575 (RIBC_BACSU) |
GO terms | GO:0016301 kinase activity
GO:0016779 nucleotidyltransferase activity
GO:0016740 transferase activity
GO:0008152 metabolic process
GO:0005524 ATP binding
GO:0016310 phosphorylation
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0008531 riboflavin kinase activity
GO:0003919 FMN adenylyltransferase activity
GO:0009398 FMN biosynthetic process
GO:0006747 FAD biosynthetic process |
Organisms for which functions have been demonstrated | Bacillus subtilis (strain 168) |
Sequence length | 316 amino acids |
FASTA sequence | >sp|P54575|RIBC_BACSU Bifunctional riboflavin kinase/FMN adenylyltransferase OS=Bacillus subtilis (strain 168) OX=224308 GN=ribC PE=3 SV=2
MKTIHITHPHHLIKEEQAKSVMALGYFDGVHLGHQKVIGTAKQIAEEKGLTLAVMTFHPHPSHVLGRDKEPKDLITPLEDKINQIEQLGTEVLYVVKFNEVFASLSPKQFIDQYIIGLNVQHAVAGFDFTYGKYGKGTMKTMPDDLDGKAGCTMVEKLTEQDKKISSSYIRTALQNGDVELANVLLGQPYFIKGIVIHGDKRGRTIGFPTANVGLNNSYIVPPTGVYAVKAEVNGEVYNGVCNIGYKPTFYEKRPEQPSIEVNLFDFNQEVYGAAIKIEWYKRIRSERKFNGIKELTEQIEKDKQEAIRYFSNLRK |
Structure Information |
PDB ID | NA |
Quaternary structure | NA |
SCOP | |
CATH | |
TM Helix Prediction | no TM helices
# sp|P54575|RIBC_BACSU Number of predicted TMHs: 0
# sp|P54575|RIBC_BACSU Exp number of AAs in TMHs: 0.06211
# sp|P54575|RIBC_BACSU Exp number, first 60 AAs: 0.00193
# sp|P54575|RIBC_BACSU Total prob of N-in: 0.06309
sp|P54575|RIBC_BACSU TMHMM2.0 outside 1 316 |
DisProt Annotation | |
Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
spP54575RIBC_BACSU_Bifun is 316 residues long, with 0 residues (0.00 %) predicted as disordered. The protein has 0 short (< 30 residues) disorder segments and 0 long (>= 30 residues) disorder segments. |
Connections to Disease |
OMIM ID | |
Function 1 |
Function description | Bifunctional riboflavin kinase |
References for function | Mack M, van Loon AP, Hohmann HP. Regulation of riboflavin biosynthesis in Bacillus subtilis is affected by the activity of the flavokinase/flavin adenine dinucleotide synthetase encoded by ribC. J Bacteriol. 1998 Feb;180(4):950-5. doi: 10.1128/JB.180.4.950-955.1998. PMID: 9473052; PMCID: PMC106977. |
E.C. number | 2.7.1.26 |
Location of functional site(s) | |
Cellular location of function | cytoplasm |
Comments | |
Function 2 |
Function description | FMN adenylyltransferase |
References for function | Mack M, van Loon AP, Hohmann HP. Regulation of riboflavin biosynthesis in Bacillus subtilis is affected by the activity of the flavokinase/flavin adenine dinucleotide synthetase encoded by ribC. J Bacteriol. 1998 Feb;180(4):950-5. doi: 10.1128/JB.180.4.950-955.1998. PMID: 9473052; PMCID: PMC106977. |
E.C. number | 2.7.7.2 |
Location of functional site(s) | |
Cellular location of function | cytoplasm |
Comments | |