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Protein

tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC

Gene

mnmC

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm5s2U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm5s2U34 to nm5s2U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm5s2U34, to form mnm5s2U34.UniRule annotation

Catalytic activityi

S-adenosyl-L-methionine + tRNA containing 5-aminomethyl-2-thiouridine = S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate.UniRule annotation

Cofactori

FADUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Oxidoreductase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

FAD, Flavoprotein, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciECOL386585:GJFA-3162-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmCUniRule annotation
Short name:
tRNA mnm(5)s(2)U biosynthesis bifunctional proteinUniRule annotation
Including the following 2 domains:
tRNA (mnm(5)s(2)U34)-methyltransferaseUniRule annotation (EC:2.1.1.61UniRule annotation)
FAD-dependent cmnm(5)s(2)U34 oxidoreductaseUniRule annotation (EC:1.5.-.-UniRule annotation)
Gene namesi
Name:mnmCUniRule annotation
Ordered Locus Names:Z3587, ECs3208
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 668668tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmCPRO_0000095014Add
BLAST

Proteomic databases

PRIDEiQ8XCQ7.

Interactioni

Protein-protein interaction databases

STRINGi155864.Z3587.

Structurei

Secondary structure

1
668
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni2 – 54Combined sources
Beta strandi11 – 133Combined sources
Beta strandi19 – 213Combined sources
Turni22 – 254Combined sources
Beta strandi26 – 294Combined sources
Turni31 – 333Combined sources
Helixi34 – 4512Combined sources
Helixi48 – 514Combined sources
Helixi52 – 543Combined sources
Beta strandi56 – 6510Combined sources
Helixi71 – 8616Combined sources
Beta strandi94 – 10310Combined sources
Helixi107 – 1148Combined sources
Helixi118 – 1203Combined sources
Helixi121 – 1299Combined sources
Beta strandi136 – 1438Combined sources
Beta strandi148 – 1558Combined sources
Helixi157 – 1604Combined sources
Helixi161 – 1633Combined sources
Helixi166 – 1683Combined sources
Beta strandi172 – 1776Combined sources
Turni182 – 1843Combined sources
Helixi186 – 1883Combined sources
Helixi191 – 20010Combined sources
Beta strandi201 – 21010Combined sources
Helixi214 – 22310Combined sources
Beta strandi225 – 2306Combined sources
Beta strandi239 – 2446Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QY6X-ray2.00A/B2-247[»]
ProteinModelPortaliQ8XCQ7.
SMRiQ8XCQ7. Positions 1-245, 265-297, 409-464.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8XCQ7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 245245tRNA (mnm(5)s(2)U34)-methyltransferaseAdd
BLAST
Regioni270 – 668399FAD-dependent cmnm(5)s(2)U34 oxidoreductaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the methyltransferase superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family.UniRule annotation
In the C-terminal section; belongs to the DAO family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CWG. Bacteria.
COG0665. LUCA.
COG4121. LUCA.
HOGENOMiHOG000218142.
KOiK15461.
OMAiKSVLCYD.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
3.50.50.60. 3 hits.
HAMAPiMF_01102. MnmC. 1 hit.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
IPR008471. MnmC-like_methylTransf.
IPR029063. SAM-dependent_MTases.
IPR023032. tRNA_MAMT_biosynth_bifunc_MnmC.
IPR017610. tRNA_S-uridine_synth_MnmC_C.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
PF05430. Methyltransf_30. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR03197. MnmC_Cterm. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8XCQ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKHYSIQPAN LEFNAEGTPV SRDFDDVYFS NDNGLEETRY VFLGGNQLEA
60 70 80 90 100
RFPEHPHPLF VVAESGFGTG LNFLTLWQAF DQFREAHPQA QLQRLHFISF
110 120 130 140 150
EKFPLTRADL ALAHQHWPEL APWAEQLQAQ WPMPLPGCHR LLLDEGRVTL
160 170 180 190 200
DLWFGDINEL ISQLDDSLNQ KVDAWFLDGF APAKNPDMWT QNLFNAMARL
210 220 230 240 250
ARPGGTLATF TSAGFVRRGL QEAGFTMQKR KGFGRKREML CGVMEQTLPL
260 270 280 290 300
PCSTPWFNRT GSSKREVAII GGGIASALLS LALLRRGWQV TLYCADEAPA
310 320 330 340 350
LGASGNRQGA LYPLLSKHDE ALNRFFSNGF TFARRLYDSL PVKFDHDWCG
360 370 380 390 400
VTQLGWDEKS QHKIAQMLSM DLPEELAVAV EANAVEQITG VTTNCSGITY
410 420 430 440 450
PQGGWLCPAE LTRNVLELAQ QQGLQIYYQY QLQDLSRKDD CWLLTFAGDQ
460 470 480 490 500
QATHSVVVLA NGHQISRFSQ TSSLPVYSVA GQVSHIPTTP ELAKLKQVLC
510 520 530 540 550
YDGYLTPQNP ANQHHCIGAS YHRGSEETAY SEDNQQQNRQ RLIDCFPHAQ
560 570 580 590 600
WAKTVDVSKK EARCGVRCAT RDHLPMVGNV PDYEATLVEY ASLAEQKDKA
610 620 630 640 650
VSAPVFDDLF MFAALGSRGL CSAPLCAEIL AAQMSDEPIP MDASTLAALN
660
PNRLWVRKLL KGKAVKAG
Length:668
Mass (Da):74,468
Last modified:August 30, 2002 - v2
Checksum:i698D0E08AD0908BF
GO

Sequence cautioni

The sequence AAG57453 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB36631 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57453.1. Different initiation.
BA000007 Genomic DNA. Translation: BAB36631.1. Different initiation.
PIRiA85874.
H91029.
RefSeqiNP_311235.2. NC_002695.1.
WP_000683769.1. NZ_LPWC01000322.1.

Genome annotation databases

EnsemblBacteriaiAAG57453; AAG57453; Z3587.
BAB36631; BAB36631; BAB36631.
GeneIDi913957.
KEGGiece:Z3587.
ecs:ECs3208.
PATRICi18355808. VBIEscCol44059_3105.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57453.1. Different initiation.
BA000007 Genomic DNA. Translation: BAB36631.1. Different initiation.
PIRiA85874.
H91029.
RefSeqiNP_311235.2. NC_002695.1.
WP_000683769.1. NZ_LPWC01000322.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QY6X-ray2.00A/B2-247[»]
ProteinModelPortaliQ8XCQ7.
SMRiQ8XCQ7. Positions 1-245, 265-297, 409-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi155864.Z3587.

Proteomic databases

PRIDEiQ8XCQ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG57453; AAG57453; Z3587.
BAB36631; BAB36631; BAB36631.
GeneIDi913957.
KEGGiece:Z3587.
ecs:ECs3208.
PATRICi18355808. VBIEscCol44059_3105.

Phylogenomic databases

eggNOGiENOG4105CWG. Bacteria.
COG0665. LUCA.
COG4121. LUCA.
HOGENOMiHOG000218142.
KOiK15461.
OMAiKSVLCYD.

Enzyme and pathway databases

BioCyciECOL386585:GJFA-3162-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ8XCQ7.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
3.50.50.60. 3 hits.
HAMAPiMF_01102. MnmC. 1 hit.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
IPR008471. MnmC-like_methylTransf.
IPR029063. SAM-dependent_MTases.
IPR023032. tRNA_MAMT_biosynth_bifunc_MnmC.
IPR017610. tRNA_S-uridine_synth_MnmC_C.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
PF05430. Methyltransf_30. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR03197. MnmC_Cterm. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMNMC_ECO57
AccessioniPrimary (citable) accession number: Q8XCQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: August 30, 2002
Last modified: September 7, 2016
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.