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Q899S1 (MNMG_CLOTE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG
Alternative name(s):
Glucose-inhibited division protein A
Gene names
Name:mnmG
Synonyms:gidA
Ordered Locus Names:CTC_00099
OrganismClostridium tetani (strain Massachusetts / E88) [Complete proteome] [HAMAP]
Taxonomic identifier212717 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length623 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm5s2U34 By similarity. HAMAP-Rule MF_00129

Cofactor

FAD By similarity. HAMAP-Rule MF_00129

Subunit structure

Homodimer By similarity. Heterotetramer of two MnmE and two MnmG subunits By similarity. HAMAP-Rule MF_00129

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00129.

Sequence similarities

Belongs to the MnmG family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
NAD
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processoxidation-reduction process

Inferred from electronic annotation. Source: InterPro

tRNA wobble uridine modification

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionflavin adenine dinucleotide binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 623623tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG HAMAP-Rule MF_00129
PRO_0000117089

Regions

Nucleotide binding14 – 196FAD By similarity
Nucleotide binding273 – 28715NAD Potential

Sequences

Sequence LengthMass (Da)Tools
Q899S1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: C9F03133AFAD667C

FASTA62369,943
        10         20         30         40         50         60 
MKYYAGDYDV VVVGAGHAGC EAALAAARIG CKVLICTISL DSVALMPCNP NIGGTAKGHL 

        70         80         90        100        110        120 
VREIDALGGE MGVNIDNTFI QSRMLNTSKG PAVHSLRAQA DKSRYSNRMK YILENEENVT 

       130        140        150        160        170        180 
LKQIEVISID IENGKVKGIL TKNGAYYNAK TVVLATGTYL NARIIIGEVA YSGGPNGLFP 

       190        200        210        220        230        240 
AKELTKNLMD LGISIRRFKT GTPARVNKKT IDFSKMIEQP GDEKIVPFSF LTDKLEREQV 

       250        260        270        280        290        300 
SCYLTYTNEN THEVIRKNLH RSPMFNGSIE GVGARYCPSI EDKVNRFPDK NKHQVFIEPE 

       310        320        330        340        350        360 
GEYTNEMYVS GLSSSLPEEI QVAMYRTVPG LENVEFLRTA YAIEYDCIDP QELKLSLESK 

       370        380        390        400        410        420 
NIEGLFSGGQ INGSSGYEEA AAQGLIAGIN AAMKVKEKDP LLLTRSDGYI GVLIDDLVTK 

       430        440        450        460        470        480 
GTNEPYRMMT SRSEYRLLLR QGNADLRLTQ KGYDVGLVSE ERYKRYINRR ESIKSEIERI 

       490        500        510        520        530        540 
KNVQITNKKE VNEFLLSLNS SELKKPISLY ELIKRPELDY YKVEQLDKGR INLPEDVQEE 

       550        560        570        580        590        600 
VNTTAKYEGY IEKQLEQVNQ FKKFENKLLP NDIDYSKVYG LRIESVQKLS KIRPMNIGQA 

       610        620 
SRISGVSPAD ISVLLIYLEH KYK 

« Hide

References

[1]"The genome sequence of Clostridium tetani, the causative agent of tetanus disease."
Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Massachusetts / E88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015927 Genomic DNA. Translation: AAO34751.1.
RefSeqNP_780814.1. NC_004557.1.

3D structure databases

ProteinModelPortalQ899S1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING212717.CTC00099.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO34751; AAO34751; CTC_00099.
GeneID1058794.
KEGGctc:CTC00099.
PATRIC19507940. VBICloTet101274_0046.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0445.
KOK03495.
OMAYINGLST.
OrthoDBEOG6W9X6J.
ProtClustDBPRK05192.

Enzyme and pathway databases

BioCycCTET212717:GJAM-51-MONOMER.

Family and domain databases

HAMAPMF_00129. MnmG_GidA.
InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004416. GidA.
IPR026904. GidA-assoc_3.
IPR002218. GIDA-rel.
IPR020595. GIDA-rel_CS.
[Graphical view]
PfamPF01134. GIDA. 1 hit.
PF13932. GIDA_assoc_3. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
TIGRFAMsTIGR00136. gidA. 1 hit.
PROSITEPS01280. GIDA_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMNMG_CLOTE
AccessionPrimary (citable) accession number: Q899S1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families