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 modification GTPase MnmE

Gene

mnmE

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

Functioni

Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm5s2U34.

Cofactori

K+Note: Binds 1 potassium ion per subunit.

Enzyme regulationi

GTPase activity is strongly activated by potassium ions.

Kineticsi

  1. KM=511 µM for GTP2 Publications
  2. KM=346 µM for XTP2 Publications
  1. Vmax=193 nmol/min/mg enzyme with GTP as substrate2 Publications
  2. Vmax=100 nmol/min/mg enzyme with XTP as substrate2 Publications

pH dependencei

Optimum pH is 7.5-9.5.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei23FormyltetrahydrofolateUniRule annotation1
Binding sitei80FormyltetrahydrofolateUniRule annotation1
Binding sitei120FormyltetrahydrofolateUniRule annotation1
Metal bindingi226Potassium1
Metal bindingi230Magnesium1
Metal bindingi245Potassium; via carbonyl oxygen1
Metal bindingi247Potassium; via carbonyl oxygen1
Metal bindingi250Potassium1
Metal bindingi251Magnesium1
Binding sitei454FormyltetrahydrofolateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi226 – 231GTP6
Nucleotide bindingi245 – 251GTP7
Nucleotide bindingi270 – 273GTP4
Nucleotide bindingi335 – 338GTP4
Nucleotide bindingi358 – 360GTP3

GO - Molecular functioni

  • GDP binding Source: EcoCyc
  • GTPase activity Source: EcoCyc
  • GTP binding Source: EcoCyc
  • potassium ion binding Source: EcoCyc

GO - Biological processi

  • chaperone-mediated protein folding Source: EcoCyc
  • response to pH Source: EcoCyc
  • tRNA methylation Source: EcoCyc
  • tRNA wobble uridine modification Source: EcoCyc
  • xenobiotic metabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyciEcoCyc:EG10997-MONOMER.
ECOL316407:JW3684-MONOMER.
MetaCyc:EG10997-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA modification GTPase MnmEUniRule annotation (EC:3.6.-.-UniRule annotation)
Gene namesi
Name:mnmEUniRule annotation
Synonyms:thdFUniRule annotation, trmEUniRule annotation
Ordered Locus Names:b3706, JW3684
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10997. mnmE.

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication

  • Note: Partially associated with the inner membrane.

GO - Cellular componenti

  • cytoplasm Source: EcoCyc
  • cytosol Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi224R → A: 1.5-fold decrease in GTPase activity and almost no change in affinity. 1 Publication1
Mutagenesisi226N → A: 100-fold decrease in GTPase activity. 5-fold decrease of affinity for GTP. 1 Publication1
Mutagenesisi226N → K: 70-fold decrease in GTPase activity. 2-fold decrease of affinity for GTP. 1 Publication1
Mutagenesisi228G → A: Loss of GTP binding and hydrolase activity. Completely impairs tRNA modifying function. 1 Publication1
Mutagenesisi249G → A: 22-fold decrease in GTPase activity and 7-fold increase of affinity. 1 Publication1
Mutagenesisi250T → A: 4-fold decrease in GTPase activity and 1.5-fold increase of affinity. 1 Publication1
Mutagenesisi250T → S: 1.8-fold decrease in GTPase activity and 1.5-fold increase of affinity. 1 Publication1
Mutagenesisi251T → A: 92-fold decrease in GTPase activity and 59-fold increase of affinity. 1 Publication1
Mutagenesisi251T → S: 4-fold decrease in GTPase activity and 1.2-fold decrease of affinity. 1 Publication1
Mutagenesisi252R → A: 7-fold decrease in GTPase activity and 6-fold increase of affinity. 1 Publication1
Mutagenesisi252R → K: 2-fold decrease in GTPase activity and no change in affinity. 1 Publication1
Mutagenesisi253D → A: 9-fold decrease in GTPase activity and 13-fold increase of affinity. 1 Publication1
Mutagenesisi255L → D: 1.5-fold decrease in affinity for GTP. 1 Publication1
Mutagenesisi256R → A: 2-fold decrease in GTPase activity and almost no change in affinity. 1 Publication1
Mutagenesisi270D → A: Does not affect GTP binding, but impairs hydrolase activity. Completely impairs tRNA modifying function. 1 Publication1
Mutagenesisi275R → A: 6-fold decrease in GTPase activity and 1.9-fold increase of affinity. 1 Publication1
Mutagenesisi282E → A: 1900-fold decrease in GTPase activity. 1 Publication1
Mutagenesisi282E → Q: 370-fold decrease in GTPase activity. 1 Publication1
Mutagenesisi288R → A: 1.7-fold decrease in GTPase activity and 1.5-fold increase of affinity. 1 Publication1
Mutagenesisi338D → N: Strong decrease in GTP binding. Does not affect hydrolase activity, but has 10-fold higher affinity for XTP than for GTP. Partially impairs tRNA modifying function. 1 Publication1
Mutagenesisi451C → S: No change in GTP binding and hydrolase activity. Does not affect association to the cell inner membrane. Completely impairs tRNA modifying function. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001888741 – 454tRNA modification GTPase MnmEAdd BLAST454

Proteomic databases

PaxDbiP25522.
PRIDEiP25522.

Interactioni

Subunit structurei

Homodimer. Heterotetramer of two MnmE and two MnmG subunits.UniRule annotation1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
mnmGP0A6U34EBI-550986,EBI-550977
pgaDP694323EBI-550986,EBI-562069

Protein-protein interaction databases

BioGridi4261522. 119 interactors.
DIPiDIP-11033N.
IntActiP25522. 23 interactors.
STRINGi511145.b3706.

Structurei

Secondary structure

1454
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi217 – 224Combined sources8
Helixi229 – 237Combined sources9
Beta strandi255 – 261Combined sources7
Beta strandi264 – 270Combined sources7
Helixi280 – 294Combined sources15
Beta strandi297 – 304Combined sources8
Turni305 – 307Combined sources3
Helixi313 – 316Combined sources4
Helixi318 – 323Combined sources6
Beta strandi330 – 335Combined sources6
Helixi337 – 340Combined sources4
Beta strandi345 – 349Combined sources5
Beta strandi352 – 356Combined sources5
Turni359 – 361Combined sources3
Helixi365 – 375Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RFLNMR-A210-377[»]
2GJ8X-ray1.70A/B/C/D216-384[»]
2GJ9X-ray2.00A/B/C/D216-384[»]
2GJAX-ray1.85A/B216-384[»]
ProteinModelPortaliP25522.
SMRiP25522.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25522.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini216 – 377TrmE-type GAdd BLAST162

Sequence similaritiesi

Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C1H. Bacteria.
COG0486. LUCA.
HOGENOMiHOG000200714.
InParanoidiP25522.
KOiK03650.
OMAiFTPRYAY.
PhylomeDBiP25522.

Family and domain databases

CDDicd04164. trmE. 1 hit.
Gene3Di1.20.120.430. 3 hits.
3.30.1360.120. 1 hit.
3.40.50.300. 2 hits.
HAMAPiMF_00379. GTPase_MnmE. 1 hit.
InterProiIPR031168. G_TrmE.
IPR018948. GTP-bd_TrmE_N.
IPR006073. GTP_binding_domain.
IPR004520. GTPase_MnmE.
IPR027368. MnmE_dom2.
IPR025867. MnmE_helical.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR027266. TrmE/GcvT_dom1.
[Graphical view]
PfamiPF01926. MMR_HSR1. 1 hit.
PF12631. MnmE_helical. 1 hit.
PF10396. TrmE_N. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR00450. mnmE_trmE_thdF. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS51709. G_TRME. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25522-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDNDTIVAQ ATPPGRGGVG ILRISGFKAR EVAETVLGKL PKPRYADYLP
60 70 80 90 100
FKDADGSVLD QGIALWFPGP NSFTGEDVLE LQGHGGPVIL DLLLKRILTI
110 120 130 140 150
PGLRIARPGE FSERAFLNDK LDLAQAEAIA DLIDASSEQA ARSALNSLQG
160 170 180 190 200
AFSARVNHLV EALTHLRIYV EAAIDFPDEE IDFLSDGKIE AQLNDVIADL
210 220 230 240 250
DAVRAEARQG SLLREGMKVV IAGRPNAGKS SLLNALAGRE AAIVTDIAGT
260 270 280 290 300
TRDVLREHIH IDGMPLHIID TAGLREASDE VERIGIERAW QEIEQADRVL
310 320 330 340 350
FMVDGTTTDA VDPAEIWPEF IARLPAKLPI TVVRNKADIT GETLGMSEVN
360 370 380 390 400
GHALIRLSAR TGEGVDVLRN HLKQSMGFDT NMEGGFLARR RHLQALEQAA
410 420 430 440 450
EHLQQGKAQL LGAWAGELLA EELRLAQQNL SEITGEFTSD DLLGRIFSSF

CIGK
Length:454
Mass (Da):49,231
Last modified:July 15, 1998 - v3
Checksum:i032211797805D2FE
GO

Sequence cautioni

The sequence AAB19981 differs from that shown.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S57109 Genomic DNA. Translation: AAB19981.1. Sequence problems.
L10328 Genomic DNA. Translation: AAA62057.1.
U00096 Genomic DNA. Translation: AAC76729.1.
AP009048 Genomic DNA. Translation: BAE77587.1.
PIRiA38160.
C65173.
RefSeqiNP_418162.1. NC_000913.3.
WP_001282346.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76729; AAC76729; b3706.
BAE77587; BAE77587; BAE77587.
GeneIDi948222.
KEGGiecj:JW3684.
eco:b3706.
PATRICi32122909. VBIEscCol129921_3830.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S57109 Genomic DNA. Translation: AAB19981.1. Sequence problems.
L10328 Genomic DNA. Translation: AAA62057.1.
U00096 Genomic DNA. Translation: AAC76729.1.
AP009048 Genomic DNA. Translation: BAE77587.1.
PIRiA38160.
C65173.
RefSeqiNP_418162.1. NC_000913.3.
WP_001282346.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RFLNMR-A210-377[»]
2GJ8X-ray1.70A/B/C/D216-384[»]
2GJ9X-ray2.00A/B/C/D216-384[»]
2GJAX-ray1.85A/B216-384[»]
ProteinModelPortaliP25522.
SMRiP25522.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261522. 119 interactors.
DIPiDIP-11033N.
IntActiP25522. 23 interactors.
STRINGi511145.b3706.

Proteomic databases

PaxDbiP25522.
PRIDEiP25522.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76729; AAC76729; b3706.
BAE77587; BAE77587; BAE77587.
GeneIDi948222.
KEGGiecj:JW3684.
eco:b3706.
PATRICi32122909. VBIEscCol129921_3830.

Organism-specific databases

EchoBASEiEB0990.
EcoGeneiEG10997. mnmE.

Phylogenomic databases

eggNOGiENOG4105C1H. Bacteria.
COG0486. LUCA.
HOGENOMiHOG000200714.
InParanoidiP25522.
KOiK03650.
OMAiFTPRYAY.
PhylomeDBiP25522.

Enzyme and pathway databases

BioCyciEcoCyc:EG10997-MONOMER.
ECOL316407:JW3684-MONOMER.
MetaCyc:EG10997-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP25522.
PROiP25522.

Family and domain databases

CDDicd04164. trmE. 1 hit.
Gene3Di1.20.120.430. 3 hits.
3.30.1360.120. 1 hit.
3.40.50.300. 2 hits.
HAMAPiMF_00379. GTPase_MnmE. 1 hit.
InterProiIPR031168. G_TrmE.
IPR018948. GTP-bd_TrmE_N.
IPR006073. GTP_binding_domain.
IPR004520. GTPase_MnmE.
IPR027368. MnmE_dom2.
IPR025867. MnmE_helical.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR027266. TrmE/GcvT_dom1.
[Graphical view]
PfamiPF01926. MMR_HSR1. 1 hit.
PF12631. MnmE_helical. 1 hit.
PF10396. TrmE_N. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR00450. mnmE_trmE_thdF. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS51709. G_TRME. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMNME_ECOLI
AccessioniPrimary (citable) accession number: P25522
Secondary accession number(s): Q2M819
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 15, 1998
Last modified: November 2, 2016
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.