General Information |
MoonProt ID | 487 |
First appeared in release | 3.0 |
Name(s) | Bifunctional riboflavin kinase/FMN adenylyltransferase; ribF |
UniProt ID | Q59263 (RIBF_CORAM) |
GO terms | GO:0003919 FMN adenylyltransferase activity
GO:0008531 riboflavin kinase activity
GO:0009231 riboflavin biosynthetic process
GO:0016740 transferase activity
GO:0016779 nucleotidyltransferase activity
GO:0016301 kinase activity
GO:0008152 metabolic process
GO:0016310 phosphorylation
GO:0003824 catalytic activity
GO:0005524 ATP binding
GO:0000166 nucleotide binding
GO:0009398 FMN biosynthetic process
GO:0006747 FAD biosynthetic process |
Organisms for which functions have been demonstrated | Corynebacterium ammoniagenes (Brevibacterium ammoniagenes) |
Sequence length | 338 amino acids |
FASTA sequence | >sp|Q59263|RIBF_CORAM Bifunctional riboflavin kinase/FMN adenylyltransferase OS=Corynebacterium ammoniagenes OX=1697 GN=ribF PE=1 SV=1
MDIWYGTAAVPKDLDNSAVTIGVFDGVHRGHQKLINATVEKAREVGAKAIMVTFDPHPVSVFLPRRAPLGITTLAERFALAESFGIDGVLVIDFTRELSGTSPEKYVEFLLEDTLHASHVVVGANFTFGENAAGTADSLRQICQSRLTVDVIDLLDDEGVRISSTTVREFLSEGDVARANWALGRHFYVTGPVVRGAGRGGKELGFPTANQYFHDTVALPADGVYAGWLTILPTEAPVSGNMEPEVAYAAAISVGTNPTFGDEQRSVESFVLDRDADLYGHDVKVEFVDHVRAMEKFDSVEQLLEVMAKDVQKTRTLLAQDVQAHKMAPETYFLQAES |
Structure Information |
PDB ID | 2X0K |
Quaternary structure | NA |
SCOP | |
CATH | |
TM Helix Prediction | no TM helices
# sp|Q59263|RIBF_CORAM Number of predicted TMHs: 0
# sp|Q59263|RIBF_CORAM Exp number of AAs in TMHs: 0.00674
# sp|Q59263|RIBF_CORAM Exp number, first 60 AAs: 0.00139
# sp|Q59263|RIBF_CORAM Total prob of N-in: 0.02225
sp|Q59263|RIBF_CORAM TMHMM2.0 outside 1 338 |
DisProt Annotation | |
Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
sp_Q59263_RIBF_CORAM_Bif is 338 residues long, with 7 residues (2.07 %) predicted as disordered. The protein has 1 short (< 30 residues) disorder segment and 0 long (>= 30 residues) disorder segments. |
Connections to Disease |
OMIM ID | |
Function 1 |
Function description | Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD |
References for function | Manstein DJ, Pai EF. Purification and characterization of FAD synthetase from Brevibacterium ammoniagenes. Journal of Biological Chemistry. 1986 Dec 5;261(34):16169-73. |
E.C. number | 2.7.1.26 |
Location of functional site(s) | |
Cellular location of function | mitochondria outer membrane |
Comments | |
Function 2 |
Function description | Corynebacterium ammoniagenes (Brevibacterium ammoniagenes) |
References for function | Collins MD. Transfer of Brevibacterium ammoniagenes (Cooke and Keith) to the Genus Corynebacterium as Corynebacterium ammoniagenes comb. nov. International Journal of Systematic and Evolutionary Microbiology. 1987 Oct 1;37(4):442-3. |
E.C. number | |
Location of functional site(s) | |
Cellular location of function | bacteria membrane |
Comments | |