| Tag | Content |
|---|
| CPLM ID | CPLM-010296 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC |
Protein Synonyms/Alias | 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 |
Gene Synonyms/Alias | yfcK; b2324; JW5380 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 102 | LHFISFEKFPLTRAD | acetylation | [1] | | 317 | ALYPLLSKHDEALNR | acetylation | [1] | | 359 | TQLGWDEKSQHKIAQ | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | 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. |
Sequence Annotation | REGION 1 245 tRNA (mnm(5)s(2)U34)-methyltransferase.
REGION 270 668 FAD-dependent cmnm(5)s(2)U34 |
Keyword | 3D-structure; Complete proteome; Cytoplasm; FAD; Flavoprotein; Methyltransferase; Multifunctional enzyme; Oxidoreductase; Reference proteome; S-adenosyl-L-methionine; Transferase; tRNA processing. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 668 AA |
Protein Sequence | MKHYSIQPAN LEFNAEGTPV SRDFDDVYFS NDNGLEETRY VFLGGNQLEV RFPEHPHPLF 60
VVAESGFGTG LNFLTLWQAF DQFREAHPQA QLQRLHFISF EKFPLTRADL ALAHQHWPEL 120
APWAEQLQAQ WPMPLPGCHR LLLDEGRVTL DLWFGDINEL TSQLDDSLNQ KVDAWFLDGF 180
APAKNPDMWT QNLFNAMARL ARPGGTLATF TSAGFVRRGL QDAGFTMQKR KGFGRKREML 240
CGVMEQTLPL PCSAPWFNRT GSSKREAAII GGGIASALLS LALLRRGWQV TLYCADEAPA 300
LGASGNRQGA LYPLLSKHDE ALNRFFSNAF TFARRFYDQL PVKFDHDWCG VTQLGWDEKS 360
QHKIAQMLSM DLPAELAVAV EANAVEQITG VATNCSGITY PQGGWLCPAE LTRNVLELAQ 420
QQGLQIYYQY QLQNLSRKDD CWLLNFAGDQ QATHSVVVLA NGHQISRFSQ TSTLPVYSVA 480
GQVSHIPTTP ELAELKQVLC YDGYLTPQNP ANQHHCIGAS YHRGSEDTAY SEDDQQQNRQ 540
RLIDCFPQAQ WAKEVDVSDK EARCGVRCAT RDHLPMVGNV PDYEATLVEY ASLAEQKDEA 600
VSAPVFDDLF MFAALGSRGL CSAPLCAEIL AAQMSDEPIP MDASTLAALN PNRLWVRKLL 660
KGKAVKAG 668 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0071949; F:FAD binding; IDA:EcoCyc. GO:0016645; F:oxidoreductase activity, acting on the CH-NH group of donors; IEA:InterPro. GO:0004808; F:tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase activity; IDA:EcoCyc. GO:0002097; P:tRNA wobble base modification; IEA:HAMAP. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |