We will be switching to the new UniProt website on Tuesday, June 28. Please explore and share your feedback.
Take me to UniProt BETA
UniProtKB - P25745 (MNMA_ECOLI)
Protein
tRNA-specific 2-thiouridylase MnmA
Gene
mnmA
Organism
Escherichia coli (strain K12)
Status
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 PublicationMiscellaneous
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
Catalytic activityi
- AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine34 in tRNA = 2-thiouridine34 in tRNA + A + AMP + diphosphate + H+ + L-cysteinyl-[protein]2 PublicationsEC:2.8.1.132 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 37 | ATP; via amide nitrogen and carbonyl oxygen | 1 | |
Active sitei | 102 | Nucleophile | 1 | |
Binding sitei | 127 | ATP; via amide nitrogen | 1 | |
Active sitei | 199 | Cysteine persulfide intermediate | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 11 – 18 | ATP | 8 |
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
Keywordsi
Molecular function | RNA-binding, Transferase, tRNA-binding |
Biological process | tRNA processing |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11344-MONOMER |
BRENDAi | 2.8.1.13, 2026 2.8.1.4, 2026 2.8.1.7, 2026 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:mnmA Synonyms:asuE, trmU, ycfB Ordered Locus Names:b1133, JW1119 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
Cytosol
- cytosol Source: EcoCyc
- sulfurtransferase complex Source: ComplexPortal
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 17 | D → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 37 | M → A: Reduces activity by 60%. 1 Publication | 1 | |
Mutagenesisi | 97 | N → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 99 | D → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 102 | C → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 107 | K → M: Reduces activity by 75%. 1 Publication | 1 | |
Mutagenesisi | 128 | H → A: Reduces activity by 90%. 1 Publication | 1 | |
Mutagenesisi | 149 | K → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 151 | Q → E: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 199 | C → A: Abolishes the incorporation of sulfur from the sulfur-relay system; loss of activity. 1 Publication | 1 | |
Mutagenesisi | 200 | F → A: Reduces activity by 60%. 1 Publication | 1 | |
Mutagenesisi | 239 | T → A: Reduces activity by 50%. 1 Publication | 1 | |
Mutagenesisi | 311 | R → A: Reduces activity by 75%. 1 Publication | 1 | |
Mutagenesisi | 344 | Q → A: Loss of activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000121588 | 1 – 368 | tRNA-specific 2-thiouridylase MnmAAdd BLAST | 368 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 102 ↔ 199 | Alternate |
Keywords - PTMi
Disulfide bondProteomic databases
jPOSTi | P25745 |
PaxDbi | P25745 |
PRIDEi | P25745 |
Interactioni
Subunit structurei
Interacts with TusE.
1 PublicationSites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 128 | Interaction with tRNA | 1 | |
Sitei | 344 | Interaction with tRNA | 1 |
Protein-protein interaction databases
BioGRIDi | 4263129, 67 interactors 850062, 1 interactor |
ComplexPortali | CPX-2145, tRNA-specific 2-thiouridylase tusE-mnmA complex |
DIPi | DIP-11035N |
IntActi | P25745, 8 interactors |
STRINGi | 511145.b1133 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P25745 |
SMRi | P25745 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P25745 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 97 – 99 | Interaction with target base in tRNA | 3 | |
Regioni | 149 – 151 | Interaction with tRNA | 3 | |
Regioni | 243 – 252 | Interaction with tRNA | 10 | |
Regioni | 311 – 312 | Interaction with tRNA | 2 |
Sequence similaritiesi
Belongs to the MnmA/TRMU family.Curated
Phylogenomic databases
eggNOGi | COG0482, Bacteria |
HOGENOMi | CLU_035188_1_0_6 |
InParanoidi | P25745 |
OMAi | AVCTGHY |
PhylomeDBi | P25745 |
Family and domain databases
CDDi | cd01998, tRNA_Me_trans, 1 hit |
Gene3Di | 2.30.30.280, 1 hit 3.40.50.620, 1 hit |
HAMAPi | MF_00144, tRNA_thiouridyl_MnmA, 1 hit |
InterProi | View protein in InterPro IPR023382, Adenine_a_hdrlase_dom IPR014729, Rossmann-like_a/b/a_fold IPR004506, tRNA-specific_2-thiouridylase |
TIGRFAMsi | TIGR00420, trmU, 1 hit |
i Sequence
Sequence statusi: Complete.
P25745-1 [UniParc]FASTAAdd to basket
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
Sequence cautioni
The sequence CAA41994 differs from that shown. Reason: Frameshift.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. |
PIRi | B64858 |
RefSeqi | NP_415651.4, NC_000913.3 WP_001297484.1, NZ_STEB01000016.1 |
Genome annotation databases
EnsemblBacteriai | AAC74217; AAC74217; b1133 BAA35955; BAA35955; BAA35955 |
GeneIDi | 66670600 945690 |
KEGGi | ecj:JW1119 eco:b1133 |
PATRICi | fig|1411691.4.peg.1133 |
Similar proteinsi
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. |
PIRi | B64858 |
RefSeqi | NP_415651.4, NC_000913.3 WP_001297484.1, NZ_STEB01000016.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2DER | X-ray | 3.10 | A/B | 1-368 | [»] | |
2DET | X-ray | 3.40 | A | 1-368 | [»] | |
2DEU | X-ray | 3.40 | A/B | 1-368 | [»] | |
AlphaFoldDBi | P25745 | |||||
SMRi | P25745 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263129, 67 interactors 850062, 1 interactor |
ComplexPortali | CPX-2145, tRNA-specific 2-thiouridylase tusE-mnmA complex |
DIPi | DIP-11035N |
IntActi | P25745, 8 interactors |
STRINGi | 511145.b1133 |
Proteomic databases
jPOSTi | P25745 |
PaxDbi | P25745 |
PRIDEi | P25745 |
Genome annotation databases
EnsemblBacteriai | AAC74217; AAC74217; b1133 BAA35955; BAA35955; BAA35955 |
GeneIDi | 66670600 945690 |
KEGGi | ecj:JW1119 eco:b1133 |
PATRICi | fig|1411691.4.peg.1133 |
Organism-specific databases
EchoBASEi | EB1320 |
Phylogenomic databases
eggNOGi | COG0482, Bacteria |
HOGENOMi | CLU_035188_1_0_6 |
InParanoidi | P25745 |
OMAi | AVCTGHY |
PhylomeDBi | P25745 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11344-MONOMER |
BRENDAi | 2.8.1.13, 2026 2.8.1.4, 2026 2.8.1.7, 2026 |
Miscellaneous databases
EvolutionaryTracei | P25745 |
PROi | PR:P25745 |
Family and domain databases
CDDi | cd01998, tRNA_Me_trans, 1 hit |
Gene3Di | 2.30.30.280, 1 hit 3.40.50.620, 1 hit |
HAMAPi | MF_00144, tRNA_thiouridyl_MnmA, 1 hit |
InterProi | View protein in InterPro IPR023382, Adenine_a_hdrlase_dom IPR014729, Rossmann-like_a/b/a_fold IPR004506, tRNA-specific_2-thiouridylase |
TIGRFAMsi | TIGR00420, trmU, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | MNMA_ECOLI | |
Accessioni | P25745Primary (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: | May 25, 2022 | |
This is version 171 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families