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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371ATP; via amide nitrogen and carbonyl oxygen
Active sitei102 – 1021Nucleophile
Binding sitei127 – 1271ATP; via amide nitrogen
Active sitei199 – 1991Cysteine persulfide intermediate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 188ATP

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171D → A: Loss of activity. 1 Publication
Mutagenesisi37 – 371M → A: Reduces activity by 60%. 1 Publication
Mutagenesisi97 – 971N → A: Loss of activity. 1 Publication
Mutagenesisi99 – 991D → A: Loss of activity. 1 Publication
Mutagenesisi102 – 1021C → A: Loss of activity. 1 Publication
Mutagenesisi107 – 1071K → M: Reduces activity by 75%. 1 Publication
Mutagenesisi128 – 1281H → A: Reduces activity by 90%. 1 Publication
Mutagenesisi149 – 1491K → A: Loss of activity. 1 Publication
Mutagenesisi151 – 1511Q → E: Loss of activity. 1 Publication
Mutagenesisi199 – 1991C → A: Abolishes the incorporation of sulfur from the sulfur-relay system; loss of activity. 1 Publication
Mutagenesisi200 – 2001F → A: Reduces activity by 60%. 1 Publication
Mutagenesisi239 – 2391T → A: Reduces activity by 50%. 1 Publication
Mutagenesisi311 – 3111R → A: Reduces activity by 75%. 1 Publication
Mutagenesisi344 – 3441Q → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 368368tRNA-specific 2-thiouridylase MnmAPRO_0000121588Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi102 ↔ 199Alternate

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP25745.
PaxDbiP25745.
PRIDEiP25745.

Interactioni

Subunit structurei

Interacts with TusE.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei128 – 1281Interaction with tRNA
Sitei344 – 3441Interaction with tRNA

Protein-protein interaction databases

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

Structurei

Secondary structure

1
368
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115Combined sources
Helixi19 – 268Combined sources
Beta strandi31 – 388Combined sources
Helixi45 – 6521Combined sources
Beta strandi69 – 735Combined sources
Helixi75 – 817Combined sources
Helixi83 – 919Combined sources
Helixi98 – 1058Combined sources
Turni106 – 1094Combined sources
Helixi110 – 1178Combined sources
Beta strandi122 – 1254Combined sources
Beta strandi131 – 1355Combined sources
Beta strandi138 – 1425Combined sources
Turni147 – 1493Combined sources
Helixi152 – 1554Combined sources
Helixi160 – 1656Combined sources
Helixi170 – 1723Combined sources
Helixi175 – 18410Combined sources
Helixi198 – 2047Combined sources
Helixi206 – 2116Combined sources
Beta strandi220 – 2234Combined sources
Beta strandi224 – 2263Combined sources
Beta strandi228 – 2314Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi259 – 2657Combined sources
Turni266 – 2694Combined sources
Beta strandi270 – 2767Combined sources
Turni280 – 2823Combined sources
Beta strandi284 – 29411Combined sources
Beta strandi302 – 31110Combined sources
Beta strandi317 – 3226Combined sources
Beta strandi325 – 3273Combined sources
Beta strandi329 – 33810Combined sources
Beta strandi344 – 3507Combined sources
Beta strandi353 – 36513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DERX-ray3.10A/B1-368[»]
2DETX-ray3.40A1-368[»]
2DEUX-ray3.40A/B1-368[»]
ProteinModelPortaliP25745.
SMRiP25745. Positions 4-368.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25745.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 993Interaction with target base in tRNA
Regioni149 – 1513Interaction with tRNA
Regioni243 – 25210Interaction with tRNA
Regioni311 – 3122Interaction with tRNA

Sequence similaritiesi

Belongs to the MnmA/TRMU family.Curated

Phylogenomic databases

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

Family and domain databases

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2DERX-ray3.10A/B1-368[»]
2DETX-ray3.40A1-368[»]
2DEUX-ray3.40A/B1-368[»]
ProteinModelPortaliP25745.
SMRiP25745. Positions 4-368.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263129. 18 interactions.
DIPiDIP-11035N.
IntActiP25745. 4 interactions.
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

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: September 7, 2016
This is version 136 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.