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Protein

tRNA modification GTPase MnmE

Gene

mnmE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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
  • identical protein binding Source: IntAct
  • 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

Keywordsi

Molecular functionHydrolase
Biological processtRNA processing
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyciEcoCyc:EG10997-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

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

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4261522, 160 interactors
DIPiDIP-11033N
IntActiP25522, 24 interactors
STRINGi316385.ECDH10B_3893

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
OMAiEFTQRAF
PhylomeDBiP25522

Family and domain databases

CDDicd04164 trmE, 1 hit
Gene3Di1.20.120.430, 2 hits
3.30.1360.120, 1 hit
HAMAPiMF_00379 GTPase_MnmE, 1 hit
InterProiView protein in InterPro
IPR031168 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
PfamiView protein in Pfam
PF01926 MMR_HSR1, 1 hit
PF12631 MnmE_helical, 1 hit
PF10396 TrmE_N, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
TIGRFAMsiTIGR00450 mnmE_trmE_thdF, 1 hit
TIGR00231 small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS51709 G_TRME, 1 hit

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
PATRICifig|1411691.4.peg.2997

Similar proteinsi

Entry informationi

Entry nameiMNME_ECOLI
AccessioniPrimary (citable) accession number: P25522
Secondary accession number(s): Q2M819
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 15, 1998
Last modified: March 28, 2018
This is version 171 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health