General Information |
MoonProt ID | 491 |
First appeared in release | 3.0 |
Name(s) | Bifunctional riboflavin kinase/FMN adenylyltransferase
Gene: ribF Synonyms:yaaC
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 | P0AG40 (RIBF_ECOLI) |
GO terms | GO:0016740 transferase activity
GO:0016779 nucleotidyltransferase activity
GO:0016301 kinase activity
GO:0008152 metabolic process
GO:0000166 nucleotide binding
GO:0016310 phosphorylation
GO:0003824 catalytic activity
GO:0005524 ATP binding
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 | Escherichia coli (strain K12) |
Sequence length | 313 amino acids |
FASTA sequence | >sp|P0AG40|RIBF_ECOLI Bifunctional riboflavin kinase/FMN adenylyltransferase OS=Escherichia coli (strain K12) OX=83333 GN=ribF PE=1 SV=1
MKLIRGIHNLSQAPQEGCVLTIGNFDGVHRGHRALLQGLQEEGRKRNLPVMVMLFEPQPL
ELFATDKAPARLTRLREKLRYLAECGVDYVLCVRFDRRFAALTAQNFISDLLVKHLRVKF
LAVGDDFRFGAGREGDFLLLQKAGMEYGFDITSTQTFCEGGVRISSTAVRQALADDNLAL
AESLLGHPFAISGRVVHGDELGRTIGFPTANVPLRRQVSPVKGVYAVEVLGLGEKPLPGV
ANIGTRPTVAGIRQQLEVHLLDVAMDLYGRHIQVVLRKKIRNEQRFASLDELKAQIARDE
LTAREFFGLTKPA |
Structure Information |
PDB ID | NA |
Quaternary structure | NA |
SCOP | |
CATH | |
TM Helix Prediction | no TM helices
# sp|P0AG40|RIBF_ECOLI Number of predicted TMHs: 0
# sp|P0AG40|RIBF_ECOLI Exp number of AAs in TMHs: 0.002
# sp|P0AG40|RIBF_ECOLI Exp number, first 60 AAs: 0.00037
# sp|P0AG40|RIBF_ECOLI Total prob of N-in: 0.01824
sp|P0AG40|RIBF_ECOLI TMHMM2.0 outside 1 313 |
DisProt Annotation | |
Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
spP0AG40RIBF_ECOLI_Bifun is 313 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 | ATP-dependent riboflavin kinase |
References for function | Kamio Y, Lin CK, Regue M, Wu HC. 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. 1985 May 10;260(9):5616-20. PMID: 2985604. |
E.C. number | 2.7.1.26 |
Location of functional site(s) | |
Cellular location of function | cytoplasm |
Comments | |
Function 2 |
Function description | FAD synthetase |
References for function | Kamio Y, Lin CK, Regue M, Wu HC. 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. 1985 May 10;260(9):5616-20. PMID: 2985604. |
E.C. number | 2.7.7.2 |
Location of functional site(s) | |
Cellular location of function | cytoplasm |
Comments | |