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Protein

tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC

Gene

mnmC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm5s2U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm5s2U34 to nm5s2U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm5s2U34, to form mnm5s2U34.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + tRNA containing 5-aminomethyl-2-thiouridine = S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate.

Cofactori

FAD2 Publications

GO - Molecular functioni

  • FAD binding Source: EcoCyc
  • oxidoreductase activity, acting on the CH-NH group of donors Source: InterPro
  • tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase activity Source: EcoCyc

GO - Biological processi

  • tRNA methylation Source: EcoCyc
  • tRNA wobble uridine modification Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Oxidoreductase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

FAD, Flavoprotein, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciEcoCyc:G7199-MONOMER.
ECOL316407:JW5380-MONOMER.
MetaCyc:G7199-MONOMER.
BRENDAi2.1.1.229. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC
Short name:
tRNA mnm(5)s(2)U biosynthesis bifunctional protein
Including the following 2 domains:
tRNA (mnm(5)s(2)U34)-methyltransferase (EC:2.1.1.61)
FAD-dependent cmnm(5)s(2)U34 oxidoreductase (EC:1.5.-.-)
Gene namesi
Name:mnmC
Synonyms:yfcK
Ordered Locus Names:b2324, JW5380
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14114. mnmC.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi64 – 641E → A: Loss of methyltransferase activity. 1 Publication
Mutagenesisi178 – 1781D → A: Strong decrease in methyltransferase activity. 1 Publication
Mutagenesisi180 – 1801F → A: Strong decrease in methyltransferase activity. 1 Publication
Mutagenesisi271 – 2711G → Q: 4-fold decrease in activity, but no change in FAD binding. 1 Publication
Mutagenesisi567 – 5671R → A: Loss of activity, but no change in FAD binding. 1 Publication
Mutagenesisi618 – 6181R → A: Loss of activity, but no change in FAD binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 668668tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmCPRO_0000095012Add
BLAST

Proteomic databases

PaxDbiP77182.
PRIDEiP77182.

Interactioni

Protein-protein interaction databases

BioGridi4261069. 5 interactions.
DIPiDIP-28058N.
IntActiP77182. 1 interaction.
STRINGi511145.b2324.

Structurei

Secondary structure

1
668
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 4510Combined sources
Helixi48 – 547Combined sources
Beta strandi57 – 659Combined sources
Helixi71 – 8616Combined sources
Beta strandi94 – 10310Combined sources
Helixi108 – 1147Combined sources
Helixi118 – 1203Combined sources
Helixi121 – 1299Combined sources
Beta strandi136 – 1438Combined sources
Turni144 – 1474Combined sources
Beta strandi148 – 1558Combined sources
Helixi157 – 1637Combined sources
Helixi166 – 1683Combined sources
Beta strandi172 – 1776Combined sources
Turni182 – 1843Combined sources
Helixi191 – 20010Combined sources
Beta strandi201 – 21010Combined sources
Helixi214 – 2229Combined sources
Beta strandi226 – 2305Combined sources
Beta strandi239 – 2435Combined sources
Helixi255 – 2573Combined sources
Beta strandi266 – 2705Combined sources
Helixi274 – 28512Combined sources
Beta strandi289 – 30012Combined sources
Helixi303 – 3053Combined sources
Beta strandi307 – 3115Combined sources
Helixi320 – 33920Combined sources
Beta strandi351 – 3544Combined sources
Helixi358 – 36912Combined sources
Turni374 – 3763Combined sources
Beta strandi378 – 3803Combined sources
Helixi382 – 3898Combined sources
Beta strandi397 – 4004Combined sources
Beta strandi404 – 4063Combined sources
Helixi408 – 42114Combined sources
Beta strandi425 – 4284Combined sources
Beta strandi432 – 4376Combined sources
Beta strandi439 – 4468Combined sources
Turni447 – 4493Combined sources
Beta strandi450 – 45910Combined sources
Helixi462 – 4643Combined sources
Turni469 – 4735Combined sources
Beta strandi477 – 48711Combined sources
Helixi492 – 4943Combined sources
Beta strandi497 – 5059Combined sources
Turni510 – 5123Combined sources
Beta strandi513 – 5186Combined sources
Helixi532 – 54514Combined sources
Helixi550 – 5534Combined sources
Beta strandi562 – 5698Combined sources
Helixi571 – 5733Combined sources
Beta strandi576 – 5816Combined sources
Helixi583 – 5886Combined sources
Helixi594 – 5963Combined sources
Beta strandi605 – 6139Combined sources
Helixi619 – 63416Combined sources
Helixi643 – 6497Combined sources
Helixi653 – 6608Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AWIX-ray3.00A/B/C/D/E/F1-668[»]
ProteinModelPortaliP77182.
SMRiP77182. Positions 35-662.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 245245tRNA (mnm(5)s(2)U34)-methyltransferaseAdd
BLAST
Regioni270 – 668399FAD-dependent cmnm(5)s(2)U34 oxidoreductaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the methyltransferase superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family.Curated
In the C-terminal section; belongs to the DAO family.Curated

Phylogenomic databases

eggNOGiENOG4105CWG. Bacteria.
COG0665. LUCA.
COG4121. LUCA.
HOGENOMiHOG000218142.
InParanoidiP77182.
KOiK15461.
OMAiKSVLCYD.
OrthoDBiEOG61P6QH.
PhylomeDBiP77182.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
3.50.50.60. 3 hits.
HAMAPiMF_01102. MnmC.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
IPR008471. MnmC-like_methylTransf.
IPR029063. SAM-dependent_MTases.
IPR023032. tRNA_MAMT_biosynth_bifunc_MnmC.
IPR017610. tRNA_S-uridine_synth_MnmC_C.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
PF05430. Methyltransf_30. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR03197. MnmC_Cterm. 1 hit.

Sequencei

Sequence statusi: Complete.

P77182-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKHYSIQPAN LEFNAEGTPV SRDFDDVYFS NDNGLEETRY VFLGGNQLEV
60 70 80 90 100
RFPEHPHPLF VVAESGFGTG LNFLTLWQAF DQFREAHPQA QLQRLHFISF
110 120 130 140 150
EKFPLTRADL ALAHQHWPEL APWAEQLQAQ WPMPLPGCHR LLLDEGRVTL
160 170 180 190 200
DLWFGDINEL TSQLDDSLNQ KVDAWFLDGF APAKNPDMWT QNLFNAMARL
210 220 230 240 250
ARPGGTLATF TSAGFVRRGL QDAGFTMQKR KGFGRKREML CGVMEQTLPL
260 270 280 290 300
PCSAPWFNRT GSSKREAAII GGGIASALLS LALLRRGWQV TLYCADEAPA
310 320 330 340 350
LGASGNRQGA LYPLLSKHDE ALNRFFSNAF TFARRFYDQL PVKFDHDWCG
360 370 380 390 400
VTQLGWDEKS QHKIAQMLSM DLPAELAVAV EANAVEQITG VATNCSGITY
410 420 430 440 450
PQGGWLCPAE LTRNVLELAQ QQGLQIYYQY QLQNLSRKDD CWLLNFAGDQ
460 470 480 490 500
QATHSVVVLA NGHQISRFSQ TSTLPVYSVA GQVSHIPTTP ELAELKQVLC
510 520 530 540 550
YDGYLTPQNP ANQHHCIGAS YHRGSEDTAY SEDDQQQNRQ RLIDCFPQAQ
560 570 580 590 600
WAKEVDVSDK EARCGVRCAT RDHLPMVGNV PDYEATLVEY ASLAEQKDEA
610 620 630 640 650
VSAPVFDDLF MFAALGSRGL CSAPLCAEIL AAQMSDEPIP MDASTLAALN
660
PNRLWVRKLL KGKAVKAG
Length:668
Mass (Da):74,434
Last modified:March 27, 2002 - v2
Checksum:iDD246362C5B6971B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75384.2.
AP009048 Genomic DNA. Translation: BAA16181.2.
PIRiB65005.
RefSeqiNP_416827.4. NC_000913.3.
WP_000683799.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75384; AAC75384; b2324.
BAA16181; BAA16181; BAA16181.
GeneIDi946800.
KEGGiecj:JW5380.
eco:b2324.
PATRICi32120021. VBIEscCol129921_2420.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75384.2.
AP009048 Genomic DNA. Translation: BAA16181.2.
PIRiB65005.
RefSeqiNP_416827.4. NC_000913.3.
WP_000683799.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AWIX-ray3.00A/B/C/D/E/F1-668[»]
ProteinModelPortaliP77182.
SMRiP77182. Positions 35-662.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261069. 5 interactions.
DIPiDIP-28058N.
IntActiP77182. 1 interaction.
STRINGi511145.b2324.

Proteomic databases

PaxDbiP77182.
PRIDEiP77182.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75384; AAC75384; b2324.
BAA16181; BAA16181; BAA16181.
GeneIDi946800.
KEGGiecj:JW5380.
eco:b2324.
PATRICi32120021. VBIEscCol129921_2420.

Organism-specific databases

EchoBASEiEB3867.
EcoGeneiEG14114. mnmC.

Phylogenomic databases

eggNOGiENOG4105CWG. Bacteria.
COG0665. LUCA.
COG4121. LUCA.
HOGENOMiHOG000218142.
InParanoidiP77182.
KOiK15461.
OMAiKSVLCYD.
OrthoDBiEOG61P6QH.
PhylomeDBiP77182.

Enzyme and pathway databases

BioCyciEcoCyc:G7199-MONOMER.
ECOL316407:JW5380-MONOMER.
MetaCyc:G7199-MONOMER.
BRENDAi2.1.1.229. 2026.

Miscellaneous databases

PROiP77182.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
3.50.50.60. 3 hits.
HAMAPiMF_01102. MnmC.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
IPR008471. MnmC-like_methylTransf.
IPR029063. SAM-dependent_MTases.
IPR023032. tRNA_MAMT_biosynth_bifunc_MnmC.
IPR017610. tRNA_S-uridine_synth_MnmC_C.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
PF05430. Methyltransf_30. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR03197. MnmC_Cterm. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    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., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Identification of a bifunctional enzyme MnmC involved in the biosynthesis of a hypermodified uridine in the wobble position of tRNA."
    Bujnicki J.M., Oudjama Y., Roovers M., Owczarek S., Caillet J., Droogmans L.
    RNA 10:1236-1242(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MNM(5)S(2)U34 BIOSYNTHESIS, COFACTOR.
  5. "Sequence-structure-function analysis of the bifunctional enzyme MnmC that catalyses the last two steps in the biosynthesis of hypermodified nucleoside mnm5s2U in tRNA."
    Roovers M., Oudjama Y., Kaminska K.H., Purta E., Caillet J., Droogmans L., Bujnicki J.M.
    Proteins 71:2076-2085(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, MUTAGENESIS OF GLU-64; ASP-178; PHE-180; GLY-271; ARG-567 AND ARG-618.

Entry informationi

Entry nameiMNMC_ECOLI
AccessioniPrimary (citable) accession number: P77182
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 27, 2002
Last modified: January 20, 2016
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.