| General Information |
| MoonProt ID | 488 |
| First appeared in release | 3.0 |
| Name(s) | ribF/mnmA; FMN adenylyltransferase; FAD pyrophorylase; FAD synthase |
| UniProt ID | Q7NBZ0 (MNMA_MYCGA) |
| GO terms | GO:0003919 FMN adenylyltransferase activity
GO:0008033 tRNA processing
GO:0008531 riboflavin kinase activity
GO:0009231 riboflavin biosynthetic process
GO:0016740 transferase activity
GO:0016783 sulfurtransferase activity
GO:0008152 metabolic process
GO:0016740 transferase activity
GO:0008033 tRNA processing
GO:0016779 nucleotidyltransferase activity
GO:0016301 kinase activity
GO:0000049 tRNA binding
GO:0016310 phosphorylation
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0005737 cytoplasm
GO:0005524 ATP binding
GO:0003723 RNA binding
GO:0008531 riboflavin kinase activity
GO:0005737 cytoplasm
GO:0016740 transferase activity
GO:0005737 cytoplasm
GO:0006400 tRNA modification
GO:0009398 FMN biosynthetic process
GO:0006747 FAD biosynthetic process |
| Organisms for which functions have been demonstrated | Mycoplasma gallisepticum |
| Sequence length | 657 amino acids |
| FASTA sequence | >sp|Q7NBZ0|MNMA_MYCGA Trifunctional protein RibF/MnmA OS=Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2)) OX=710127 GN=ribF/mnmA PE=3 SV=1
MLSIINLTSKTIKEVNKGVDLVIGFFDGIHKGHAKLFKQSDRFNLLTFDHIPKKQRLLYPKVDEIEQLSALSGLEQLLVYDLLNNNLSAQEFIDNYIKLIQPKRIIVGSDFKFGSDQVDYSLFAKNGYEVVVVKKDHCSTSEIKKLIINCDLDQANKLLLTPFYLKGTVIKNAQRGRTIGFVTANIILDNQLIELTEGSYVCKVIVDNKTYQGICFIGKPKTFDEKQRQCEAHIFDFDQDIYGKKIKVELYQFIRPTVKFNSINELKEAIENDKKAALSFFHKQEKPKVVVALSGGVDSAVCAYLLQQQGYDVVAAFMQNWDKDLNFELLSDHADDQIQGCDAKQDYEDTQKLCEQLKIKLYHFNFVEQYWNDVFLKVLEDYKKGLTPNPDVLCNQFGKFGWFINALRKQFGDDIKIAFGHYAKLITKDDEVFLVHTKDHNKDQTYFLTMLKKEQLKNIIFPLSELDKPTVREIAKQANLYVANKKDSTGICFIGERNFKQFLSNYLAIKKGPIILIDENKKIGEHDGLYFYTIGQSRRLHVGGTKEKIFVCDKDYNNNTLYVCYESSKDQYLSSVSCELEKFNWLIDTKDQLFNKKLWIRFRHRQKLQECEIVSYHDDKVIVKYTKQIGVTPGQYGVIYDQNLWVVGGGKITKIIK |
| Structure Information |
| PDB ID | NA |
| Quaternary structure | NA |
| SCOP | |
| CATH | |
| TM Helix Prediction | no TM helices
# sp|Q7NBZ0|MNMA_MYCGA Number of predicted TMHs: 0
# sp|Q7NBZ0|MNMA_MYCGA Exp number of AAs in TMHs: 0.01083
# sp|Q7NBZ0|MNMA_MYCGA Exp number, first 60 AAs: 0.00053
# sp|Q7NBZ0|MNMA_MYCGA Total prob of N-in: 0.00059
sp|Q7NBZ0|MNMA_MYCGA TMHMM2.0 outside 1 657 |
| DisProt Annotation | |
| Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
sp_Q7NBZ0_MNMA_MYCGA_Tri is 657 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 | 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 inner membrane |
| Comments | ATP + FMN + H+ = diphosphate + FAD,
EC:2.7.1.26 |
| Function 2 |
| Function description | FMN adenylyltransferase |
| References for function | Huerta C, Borek D, Machius M, Grishin NV, Zhang H. Structure and mechanism of a eukaryotic FMN adenylyltransferase. Journal of molecular biology. 2009 Jun 5;389(2):388-400. |
| E.C. number | 2.7.7.2 |
| Location of functional site(s) | |
| Cellular location of function | mitochondria inner membrane |
| Comments | ATP + riboflavin = ADP + FMN + H+,
EC: 2.7.7.2 |