| General Information |
| MoonProt ID | 489 |
| First appeared in release | 3.0 |
| Name(s) | Riboflavin biosynthesis protein; ribD |
| UniProt ID | P25539 (RIBD_ECOLI) |
| GO terms | GO:0008835 diaminohydroxyphosphoribosylaminopyrimidine deaminase activity
GO:0008270 zinc ion binding
GO:0009231 riboflavin biosynthetic process
GO:0016787 hydrolase activity
GO:0050661 NADP binding
GO:0055114 oxidation-reduction process
GO:0003824 catalytic activity
GO:0008703 5-amino-6-(5-phosphoribosylamino)uracil reductase activity
GO:0008152 metabolic process
GO:0046872 metal ion binding
GO:0016491 oxidoreductase activity
GO:0003824 catalytic activity
GO:0005515 protein binding |
| Organisms for which functions have been demonstrated | Escherichia coli (strain K12) |
| Sequence length | 367 amino acids |
| FASTA sequence | >sp|P25539|RIBD_ECOLI Riboflavin biosynthesis protein RibD OS=Escherichia coli (strain K12) OX=83333 GN=ribD PE=1 SV=1
MQDEYYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTPPCCDALIAAGVARVVASMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEQLNKGFLKRMRTGFPYIQLKLGASLDGRTAMASGESQWITSPQARRDVQLLRAQSHAILTSSATVLADDPALTVRWSELDEQTQALYPQQNLRQPIRIVIDSQNRVTPVHRIVQQPGETWFARTQEDSREWPETVRTLLIPEHKGHLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDELIVYIAPKLLGSDARGLCTLPGLEKLADAPQFKFKEIRHVGPDVCLHLVGA |
| Structure Information |
| PDB ID | 2G6V, 2O7P, 2OBC |
| Quaternary structure | homodimer |
| SCOP | |
| CATH | |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | |
| Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
sp_P25539_RIBD_ECOLI_Rib is 367 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 | RibD diaminohydroxyphosphoribosylaminopyrimidine deaminase |
| References for function | Schomburg D, Salzmann M. Diaminohydroxyphosphoribosylaminopyrimidine deaminase. InEnzyme Handbook 4 1991 (pp. 1095-1097). Springer, Berlin, Heidelberg. |
| E.C. number | 3.5.4.26 |
| Location of functional site(s) | |
| Cellular location of function | |
| Comments | |
| Function 2 |
| Function description | 5-amino-6-(5-phosphoribosylamino)uracil reductase |
| References for function | 1.1.1.193 |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | |
| Comments | |