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Protein

tRNA-specific 2-thiouridylase MnmA

Gene

mnmA

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

Functioni

Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation of s2U34, the first step of tRNA-mnm5s2U34 synthesis. Sulfur is provided by IscS, via a sulfur-relay system. Binds ATP and its substrate tRNAs.1 Publication

Catalytic activityi

A [protein]-S-sulfanyl-L-cysteine + uridine(34) in tRNA + ATP + reduced acceptor = a [protein]-L-cysteine + 2-thiouridine(34) in tRNA + AMP + diphosphate + acceptor.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei37ATP; via amide nitrogen and carbonyl oxygen1
Active sitei102Nucleophile1
Binding sitei127ATP; via amide nitrogen1
Active sitei199Cysteine persulfide intermediate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 18ATP8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • sulfurtransferase activity Source: EcoCyc
  • tRNA binding Source: UniProtKB-KW

GO - Biological processi

  • tRNA wobble position uridine thiolation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11344-MONOMER.
ECOL316407:JW1119-MONOMER.
MetaCyc:EG11344-MONOMER.
BRENDAi2.8.1.4. 2026.
2.8.1.7. 2026.
2.8.1.B1. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-specific 2-thiouridylase MnmA (EC:2.8.1.132 Publications)
Gene namesi
Name:mnmA
Synonyms:asuE, trmU, ycfB
Ordered Locus Names:b1133, JW1119
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11344. mnmA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi17D → A: Loss of activity. 1 Publication1
Mutagenesisi37M → A: Reduces activity by 60%. 1 Publication1
Mutagenesisi97N → A: Loss of activity. 1 Publication1
Mutagenesisi99D → A: Loss of activity. 1 Publication1
Mutagenesisi102C → A: Loss of activity. 1 Publication1
Mutagenesisi107K → M: Reduces activity by 75%. 1 Publication1
Mutagenesisi128H → A: Reduces activity by 90%. 1 Publication1
Mutagenesisi149K → A: Loss of activity. 1 Publication1
Mutagenesisi151Q → E: Loss of activity. 1 Publication1
Mutagenesisi199C → A: Abolishes the incorporation of sulfur from the sulfur-relay system; loss of activity. 1 Publication1
Mutagenesisi200F → A: Reduces activity by 60%. 1 Publication1
Mutagenesisi239T → A: Reduces activity by 50%. 1 Publication1
Mutagenesisi311R → A: Reduces activity by 75%. 1 Publication1
Mutagenesisi344Q → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001215881 – 368tRNA-specific 2-thiouridylase MnmAAdd BLAST368

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi102 ↔ 199Alternate

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP25745.
PaxDbiP25745.
PRIDEiP25745.

Interactioni

Subunit structurei

Interacts with TusE.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei128Interaction with tRNA1
Sitei344Interaction with tRNA1

Protein-protein interaction databases

BioGridi4263129. 18 interactors.
DIPiDIP-11035N.
IntActiP25745. 4 interactors.
STRINGi511145.b1133.

Structurei

Secondary structure

1368
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Helixi19 – 26Combined sources8
Beta strandi31 – 38Combined sources8
Helixi45 – 65Combined sources21
Beta strandi69 – 73Combined sources5
Helixi75 – 81Combined sources7
Helixi83 – 91Combined sources9
Helixi98 – 105Combined sources8
Turni106 – 109Combined sources4
Helixi110 – 117Combined sources8
Beta strandi122 – 125Combined sources4
Beta strandi131 – 135Combined sources5
Beta strandi138 – 142Combined sources5
Turni147 – 149Combined sources3
Helixi152 – 155Combined sources4
Helixi160 – 165Combined sources6
Helixi170 – 172Combined sources3
Helixi175 – 184Combined sources10
Helixi198 – 204Combined sources7
Helixi206 – 211Combined sources6
Beta strandi220 – 223Combined sources4
Beta strandi224 – 226Combined sources3
Beta strandi228 – 231Combined sources4
Beta strandi252 – 254Combined sources3
Beta strandi259 – 265Combined sources7
Turni266 – 269Combined sources4
Beta strandi270 – 276Combined sources7
Turni280 – 282Combined sources3
Beta strandi284 – 294Combined sources11
Beta strandi302 – 311Combined sources10
Beta strandi317 – 322Combined sources6
Beta strandi325 – 327Combined sources3
Beta strandi329 – 338Combined sources10
Beta strandi344 – 350Combined sources7
Beta strandi353 – 365Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DERX-ray3.10A/B1-368[»]
2DETX-ray3.40A1-368[»]
2DEUX-ray3.40A/B1-368[»]
ProteinModelPortaliP25745.
SMRiP25745.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25745.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni97 – 99Interaction with target base in tRNA3
Regioni149 – 151Interaction with tRNA3
Regioni243 – 252Interaction with tRNA10
Regioni311 – 312Interaction with tRNA2

Sequence similaritiesi

Belongs to the MnmA/TRMU family.Curated

Phylogenomic databases

eggNOGiENOG4105CCJ. Bacteria.
COG0482. LUCA.
HOGENOMiHOG000218046.
InParanoidiP25745.
KOiK00566.
OMAiLHKINFA.
PhylomeDBiP25745.

Family and domain databases

CDDicd01998. tRNA_Me_trans. 1 hit.
Gene3Di2.30.30.280. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00144. tRNA_thiouridyl_MnmA. 1 hit.
InterProiIPR023382. Adenine_a_hdrlase_dom.
IPR014729. Rossmann-like_a/b/a_fold.
IPR004506. tRNA-specific_2-thiouridylase.
[Graphical view]
PANTHERiPTHR11933. PTHR11933. 1 hit.
TIGRFAMsiTIGR00420. trmU. 1 hit.

Sequencei

Sequence statusi: Complete.

P25745-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSETAKKVIV GMSGGVDSSV SAWLLQQQGY QVEGLFMKNW EEDDGEEYCT
60 70 80 90 100
AAADLADAQA VCDKLGIELH TVNFAAEYWD NVFELFLAEY KAGRTPNPDI
110 120 130 140 150
LCNKEIKFKA FLEFAAEDLG ADYIATGHYV RRADVDGKSR LLRGLDSNKD
160 170 180 190 200
QSYFLYTLSH EQIAQSLFPV GELEKPQVRK IAEDLGLVTA KKKDSTGICF
210 220 230 240 250
IGERKFREFL GRYLPAQPGK IITVDGDEIG EHQGLMYHTL GQRKGLGIGG
260 270 280 290 300
TKEGTEEPWY VVDKDVENNI LVVAQGHEHP RLMSVGLIAQ QLHWVDREPF
310 320 330 340 350
TGTMRCTVKT RYRQTDIPCT VKALDDDRIE VIFDEPVAAV TPGQSAVFYN
360
GEVCLGGGII EQRLPLPV
Length:368
Mass (Da):40,959
Last modified:May 30, 2000 - v4
Checksum:i22CA92676D0805CC
GO

Sequence cautioni

The sequence CAA41994 differs from that shown. Reason: Frameshift at positions 175 and 215.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74217.2.
AP009048 Genomic DNA. Translation: BAA35955.1.
X59307 Genomic DNA. Translation: CAA41994.1. Frameshift.
M74924 Genomic DNA. No translation available.
PIRiB64858.
RefSeqiNP_415651.4. NC_000913.3.
WP_001297484.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74217; AAC74217; b1133.
BAA35955; BAA35955; BAA35955.
GeneIDi945690.
KEGGiecj:JW1119.
eco:b1133.
PATRICi32117515. VBIEscCol129921_1180.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74217.2.
AP009048 Genomic DNA. Translation: BAA35955.1.
X59307 Genomic DNA. Translation: CAA41994.1. Frameshift.
M74924 Genomic DNA. No translation available.
PIRiB64858.
RefSeqiNP_415651.4. NC_000913.3.
WP_001297484.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DERX-ray3.10A/B1-368[»]
2DETX-ray3.40A1-368[»]
2DEUX-ray3.40A/B1-368[»]
ProteinModelPortaliP25745.
SMRiP25745.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263129. 18 interactors.
DIPiDIP-11035N.
IntActiP25745. 4 interactors.
STRINGi511145.b1133.

Proteomic databases

EPDiP25745.
PaxDbiP25745.
PRIDEiP25745.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74217; AAC74217; b1133.
BAA35955; BAA35955; BAA35955.
GeneIDi945690.
KEGGiecj:JW1119.
eco:b1133.
PATRICi32117515. VBIEscCol129921_1180.

Organism-specific databases

EchoBASEiEB1320.
EcoGeneiEG11344. mnmA.

Phylogenomic databases

eggNOGiENOG4105CCJ. Bacteria.
COG0482. LUCA.
HOGENOMiHOG000218046.
InParanoidiP25745.
KOiK00566.
OMAiLHKINFA.
PhylomeDBiP25745.

Enzyme and pathway databases

BioCyciEcoCyc:EG11344-MONOMER.
ECOL316407:JW1119-MONOMER.
MetaCyc:EG11344-MONOMER.
BRENDAi2.8.1.4. 2026.
2.8.1.7. 2026.
2.8.1.B1. 2026.

Miscellaneous databases

EvolutionaryTraceiP25745.
PROiP25745.

Family and domain databases

CDDicd01998. tRNA_Me_trans. 1 hit.
Gene3Di2.30.30.280. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00144. tRNA_thiouridyl_MnmA. 1 hit.
InterProiIPR023382. Adenine_a_hdrlase_dom.
IPR014729. Rossmann-like_a/b/a_fold.
IPR004506. tRNA-specific_2-thiouridylase.
[Graphical view]
PANTHERiPTHR11933. PTHR11933. 1 hit.
TIGRFAMsiTIGR00420. trmU. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMNMA_ECOLI
AccessioniPrimary (citable) accession number: P25745
Secondary accession number(s): P75964
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 30, 2000
Last modified: November 2, 2016
This is version 138 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

During the reaction, ATP is used to activate the C2 atom of U34 by adenylation. After this, the persulfide sulfur on the catalytic cysteine is transferred to the C2 atom of U34. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards the activated C2 atom on U34. Subsequently, Cys-102 acts as nucleophile towards Cys-199, and a transient disulfide bond is formed.

Caution

Was originally thought to be a 5-methylaminomethyl-2-methyltransferase involved in tRNA modification.Curated

Keywords - Technical termi

3D-structure, Complete proteome, 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

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.