Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi64E → A: Loss of methyltransferase activity. 1 Publication1
Mutagenesisi178D → A: Strong decrease in methyltransferase activity. 1 Publication1
Mutagenesisi180F → A: Strong decrease in methyltransferase activity. 1 Publication1
Mutagenesisi271G → Q: 4-fold decrease in activity, but no change in FAD binding. 1 Publication1
Mutagenesisi567R → A: Loss of activity, but no change in FAD binding. 1 Publication1
Mutagenesisi618R → A: Loss of activity, but no change in FAD binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000950121 – 668tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmCAdd BLAST668

Proteomic databases

PaxDbiP77182.
PRIDEiP77182.

Interactioni

Protein-protein interaction databases

BioGridi4261069. 5 interactors.
DIPiDIP-28058N.
IntActiP77182. 1 interactor.
STRINGi511145.b2324.

Structurei

Secondary structure

1668
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 45Combined sources10
Helixi48 – 54Combined sources7
Beta strandi57 – 65Combined sources9
Helixi71 – 86Combined sources16
Beta strandi94 – 103Combined sources10
Helixi108 – 114Combined sources7
Helixi118 – 120Combined sources3
Helixi121 – 129Combined sources9
Beta strandi136 – 143Combined sources8
Turni144 – 147Combined sources4
Beta strandi148 – 155Combined sources8
Helixi157 – 163Combined sources7
Helixi166 – 168Combined sources3
Beta strandi172 – 177Combined sources6
Turni182 – 184Combined sources3
Helixi191 – 200Combined sources10
Beta strandi201 – 210Combined sources10
Helixi214 – 222Combined sources9
Beta strandi226 – 230Combined sources5
Beta strandi239 – 243Combined sources5
Helixi255 – 257Combined sources3
Beta strandi266 – 270Combined sources5
Helixi274 – 285Combined sources12
Beta strandi289 – 300Combined sources12
Helixi303 – 305Combined sources3
Beta strandi307 – 311Combined sources5
Helixi320 – 339Combined sources20
Beta strandi351 – 354Combined sources4
Helixi358 – 369Combined sources12
Turni374 – 376Combined sources3
Beta strandi378 – 380Combined sources3
Helixi382 – 389Combined sources8
Beta strandi397 – 400Combined sources4
Beta strandi404 – 406Combined sources3
Helixi408 – 421Combined sources14
Beta strandi425 – 428Combined sources4
Beta strandi432 – 437Combined sources6
Beta strandi439 – 446Combined sources8
Turni447 – 449Combined sources3
Beta strandi450 – 459Combined sources10
Helixi462 – 464Combined sources3
Turni469 – 473Combined sources5
Beta strandi477 – 487Combined sources11
Helixi492 – 494Combined sources3
Beta strandi497 – 505Combined sources9
Turni510 – 512Combined sources3
Beta strandi513 – 518Combined sources6
Helixi532 – 545Combined sources14
Helixi550 – 553Combined sources4
Beta strandi562 – 569Combined sources8
Helixi571 – 573Combined sources3
Beta strandi576 – 581Combined sources6
Helixi583 – 588Combined sources6
Helixi594 – 596Combined sources3
Beta strandi605 – 613Combined sources9
Helixi619 – 634Combined sources16
Helixi643 – 649Combined sources7
Helixi653 – 660Combined sources8

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 245tRNA (mnm(5)s(2)U34)-methyltransferaseAdd BLAST245
Regioni270 – 668FAD-dependent cmnm(5)s(2)U34 oxidoreductaseAdd BLAST399

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.
PhylomeDBiP77182.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
3.50.50.60. 3 hits.
HAMAPiMF_01102. MnmC. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AWIX-ray3.00A/B/C/D/E/F1-668[»]
ProteinModelPortaliP77182.
SMRiP77182.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261069. 5 interactors.
DIPiDIP-28058N.
IntActiP77182. 1 interactor.
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.
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. 1 hit.
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...

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: November 2, 2016
This is version 127 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.