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A9VTL9 (MNMG_BACWK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:BcerKBAB4_5276
OrganismBacillus weihenstephanensis (strain KBAB4) [Complete proteome] [HAMAP]
Taxonomic identifier315730 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length629 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_processtRNA 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 – 629629tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG HAMAP-Rule MF_00129
PRO_0000345241

Regions

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

Sites

Binding site1261FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1811FAD By similarity
Binding site3701FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A9VTL9 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: ACFC8F5C64E6FC3C

FASTA62970,164
        10         20         30         40         50         60 
MGYNAGSYDV IVIGAGHAGC EAGLAAARMG SKTLMLTINL DMVAFMPCNP SVGGPAKGIV 

        70         80         90        100        110        120 
VREIDALGGE MGRNIDKTHI QMRMLNTGKG PAVRALRAQA DKFSYQHELK KTIEETPNLT 

       130        140        150        160        170        180 
LFQGLVERLI IEDGVCKGVI TQAGAEYTAK TVVITTGTFL RGEIIMGDLK YSSGPNNQQP 

       190        200        210        220        230        240 
SITLSEHLEE LGFDLVRFKT GTPPRVNSNT IDYSKTEIQP GDDKPRAFSF ETTKFIMDQI 

       250        260        270        280        290        300 
PCWLTYTSTE THRLIDENLH RSAMYSGMIK GTGPRYCPSI EDKVVRFNDK PRHQIFLEPE 

       310        320        330        340        350        360 
GRNTQEVYVQ GLSTSLPEDV QRAMLRTIPG LENVEMMRTG YAIEYDAIVP TQLWPTLETK 

       370        380        390        400        410        420 
KIKNLYTAGQ INGTSGYEEA AGQGLMAGIN AACRSLGKKE VILGRADAYI GVLIDDLVTK 

       430        440        450        460        470        480 
GTNEPYRLLT SRAEYRLLLR HDNADLRLTE VGREIGLIKE DRYERFTNKK LQIEQEKERL 

       490        500        510        520        530        540 
ESIFIKPRPE VQELIRSIGG SELKDGIRAS DLLRRPEVTY EHIHLLVPSE VALSDEITEQ 

       550        560        570        580        590        600 
VEIQTKYEGY IEKSLQQVER MKKMENKKIP VDIDYDAISS LASEARQKLK DVRPLSMGQA 

       610        620 
SRISGVNPAD VSILLIYIEQ GKIARVSNQ 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KBAB4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000903 Genomic DNA. Translation: ABY46419.1.
RefSeqYP_001648047.1. NC_010184.1.

3D structure databases

ProteinModelPortalA9VTL9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING315730.BcerKBAB4_5276.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY46419; ABY46419; BcerKBAB4_5276.
GeneID5845521.
KEGGbwe:BcerKBAB4_5276.
PATRIC19015324. VBIBacWei55973_5944.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0445.
HOGENOMHOG000201059.
KOK03495.
OMAHTNEQTH.
OrthoDBEOG6W9X6J.

Enzyme and pathway databases

BioCycBWEI315730:GHRU-5424-MONOMER.

Family and domain databases

HAMAPMF_00129. MnmG_GidA.
InterProIPR004416. 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]
TIGRFAMsTIGR00136. gidA. 1 hit.
PROSITEPS01280. GIDA_1. 1 hit.
PS01281. GIDA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMNMG_BACWK
AccessionPrimary (citable) accession number: A9VTL9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 45 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