tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein mnmC (P77182)

Identification
Name:tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein mnmC
Synonyms:
  • tRNA mnm(5)s(2)U biosynthesis bifunctional protein
  • tRNA (mnm(5)s(2)U34)-methyltransferase
  • FAD-dependent cmnm(5)s(2)U34 oxidoreductase
Gene Name:mnmC
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity
Specific Function:Catalyzes the last two steps in the biosynthesis of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34
Cellular Location:Cytoplasm (Potential)
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
KEGG Reactions:
1.0Thumb+1.0tRNA containing 5-aminomethyl-2-thiouridine ↔ 1.0Thumb+1.0tRNA containing 5-methylaminomethyl-2-thiouridylate
1.0S-Adenosylmethionine + 1.0tRNA containing 5-aminomethyl-2-thiouridine ↔ 1.0S-Adenosylhomocysteine + 1.0tRNA containing 5-methylaminomethyl-2-thiouridylate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00939S-AdenosylhomocysteineMetaboCard
GO Classification:
Function
catalytic activity
methyltransferase activity
oxidoreductase activity
oxidoreductase activity, acting on the CH-NH group of donors
transferase activity
transferase activity, transferring one-carbon groups
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b2324
Gene OrientationClockwise
Centisome Percentage:52.59
Left Sequence End2439786
Right Sequence End2441792
Gene Sequence:
>2007 bp
GTGAAACACTACTCCATACAACCTGCCAACCTCGAATTTAATGCTGAGGGTACACCTGTT
TCCCGAGATTTTGACGATGTCTATTTTTCCAACGATAACGGGCTGGAAGAGACGCGTTAT
GTTTTTCTGGGAGGCAACCAATTAGAGGTACGCTTTCCTGAGCATCCACATCCTCTGTTT
GTGGTAGCAGAGAGCGGCTTCGGCACCGGATTAAACTTCCTGACGCTATGGCAGGCATTT
GATCAGTTTCGCGAAGCGCATCCGCAAGCGCAATTACAACGCTTACATTTCATTAGTTTT
GAGAAATTTCCCCTCACCCGTGCGGATTTAGCCTTAGCGCATCAACACTGGCCGGAACTG
GCTCCGTGGGCAGAACAACTTCAGGCGCAGTGGCCAATGCCCTTGCCCGGTTGCCATCGT
TTATTGCTCGATGAAGGCCGCGTGACGCTGGATTTATGGTTTGGCGATATTAACGAACTG
ACCAGCCAACTGGACGATTCGCTAAATCAAAAAGTAGATGCCTGGTTTCTGGACGGCTTT
GCGCCAGCGAAAAACCCGGATATGTGGACGCAAAATCTGTTTAACGCCATGGCAAGGTTG
GCGCGTCCGGGCGGCACGCTGGCGACATTTACGTCTGCCGGTTTTGTCCGCCGCGGTTTG
CAGGACGCCGGATTCACGATGCAAAAACGTAAGGGCTTTGGGCGCAAACGGGAAATGCTT
TGCGGGGTGATGGAACAGACATTACCGCTCCCCTGCTCCGCGCCGTGGTTTAACCGCACG
GGCAGCAGCAAACGGGAAGCGGCGATTATCGGCGGTGGTATTGCCAGCGCGTTGTTGTCG
CTGGCGCTATTACGGCGCGGCTGGCAGGTAACGCTTTATTGCGCGGATGAGGCCCCCGCA
CTGGGTGCTTCCGGCAATCGCCAGGGGGCGCTGTATCCGTTATTAAGCAAACACGATGAG
GCGCTAAACCGCTTTTTCTCTAATGCGTTTACTTTTGCTCGTCGGTTTTACGACCAATTA
CCCGTTAAATTTGATCATGACTGGTGCGGCGTCACGCAGTTAGGCTGGGATGAGAAAAGC
CAGCATAAAATCGCACAGATGTTGTCAATGGATTTACCCGCAGAACTGGCTGTAGCCGTT
GAGGCAAATGCGGTTGAACAAATTACGGGCGTTGCGACAAATTGCAGCGGCATTACTTAT
CCGCAAGGTGGTTGGCTGTGCCCAGCAGAACTGACCCGTAATGTGCTGGAACTGGCGCAA
CAGCAGGGTTTGCAGATTTATTATCAATATCAGTTACAGAATTTATCCCGTAAGGATGAC
TGTTGGTTGTTGAATTTTGCAGGAGATCAGCAAGCAACACACAGCGTAGTGGTACTGGCG
AACGGGCATCAAATCAGCCGATTCAGCCAAACGTCGACTCTCCCGGTGTATTCGGTTGCC
GGGCAGGTCAGCCATATTCCGACAACGCCGGAATTGGCAGAGCTGAAGCAGGTGCTGTGC
TATGACGGTTATCTCACGCCACAAAATCCGGCGAATCAACATCATTGTATTGGTGCCAGT
TATCATCGCGGCAGCGAAGATACGGCGTACAGTGAGGACGATCAGCAGCAGAATCGCCAG
CGGTTGATTGATTGTTTCCCGCAGGCACAGTGGGCAAAAGAGGTTGATGTCAGTGATAAA
GAGGCGCGCTGCGGTGTGCGTTGTGCCACCCGCGATCATCTGCCAATGGTAGGCAATGTT
CCCGATTATGAGGCAACACTCGTGGAATATGCGTCGTTGGCGGAGCAGAAAGATGAGGCG
GTAAGCGCGCCGGTTTTTGACGATCTCTTTATGTTTGCGGCTTTAGGTTCTCGCGGTTTG
TGTTCTGCCCCGCTGTGTGCCGAGATTCTGGCGGCGCAGATGAGCGACGAACCGATTCCG
ATGGATGCCAGTACGCTGGCGGCGTTAAACCCGAATCGGTTATGGGTGCGGAAATTGTTG
AAGGGTAAAGCGGTTAAGGCGGGGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:668
Protein Molecular Weight:74434
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein mnmC
MKHYSIQPANLEFNAEGTPVSRDFDDVYFSNDNGLEETRYVFLGGNQLEVRFPEHPHPLF
VVAESGFGTGLNFLTLWQAFDQFREAHPQAQLQRLHFISFEKFPLTRADLALAHQHWPEL
APWAEQLQAQWPMPLPGCHRLLLDEGRVTLDLWFGDINELTSQLDDSLNQKVDAWFLDGF
APAKNPDMWTQNLFNAMARLARPGGTLATFTSAGFVRRGLQDAGFTMQKRKGFGRKREML
CGVMEQTLPLPCSAPWFNRTGSSKREAAIIGGGIASALLSLALLRRGWQVTLYCADEAPA
LGASGNRQGALYPLLSKHDEALNRFFSNAFTFARRFYDQLPVKFDHDWCGVTQLGWDEKS
QHKIAQMLSMDLPAELAVAVEANAVEQITGVATNCSGITYPQGGWLCPAELTRNVLELAQ
QQGLQIYYQYQLQNLSRKDDCWLLNFAGDQQATHSVVVLANGHQISRFSQTSTLPVYSVA
GQVSHIPTTPELAELKQVLCYDGYLTPQNPANQHHCIGASYHRGSEDTAYSEDDQQQNRQ
RLIDCFPQAQWAKEVDVSDKEARCGVRCATRDHLPMVGNVPDYEATLVEYASLAEQKDEA
VSAPVFDDLFMFAALGSRGLCSAPLCAEILAAQMSDEPIPMDASTLAALNPNRLWVRKLL
KGKAVKAG
References
External Links:
ResourceLink
Uniprot ID:P77182
Uniprot Name:MNMC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675355
Ecogene ID:EG14114
Ecocyc:EG14114
ColiBase:b2324
Kegg Gene:b2324
EchoBASE ID:EB3867
CCDB:MNMC_ECOLI
BacMap:90111418
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Bujnicki, J. M., Oudjama, Y., Roovers, M., Owczarek, S., Caillet, J., Droogmans, L. (2004). "Identification of a bifunctional enzyme MnmC involved in the biosynthesis of a hypermodified uridine in the wobble position of tRNA." RNA 10:1236-1242. Pubmed: 15247431
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Roovers, M., Oudjama, Y., Kaminska, K. H., Purta, E., Caillet, J., Droogmans, L., Bujnicki, J. M. (2008). "Sequence-structure-function analysis of the bifunctional enzyme MnmC that catalyses the last two steps in the biosynthesis of hypermodified nucleoside mnm5s2U in tRNA." Proteins 71:2076-2085. Pubmed: 18186482
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837