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B0JGQ4 (MNMG_MICAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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:MAE_54980
OrganismMicrocystis aeruginosa (strain NIES-843) [Complete proteome] [HAMAP]
Taxonomic identifier449447 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesMicrocystis

Protein attributes

Sequence length635 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 – 635635tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG HAMAP-Rule MF_00129
PRO_1000076322

Regions

Nucleotide binding19 – 246FAD By similarity
Nucleotide binding280 – 29415NAD Potential

Sequences

Sequence LengthMass (Da)Tools
B0JGQ4 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 18CB527A00C8EDF3

FASTA63570,699
        10         20         30         40         50         60 
MTFSSAADFQ DEFDVIVVGA GHSGCEAALA CARLGCRTLL LTLNLDKIAW QPCNPAVGGP 

        70         80         90        100        110        120 
AKSQLTHEVD ALGGEIGKMA DRTYLQKRVL NASRGPAVWA LRAQTDKREY AAVMKGIVET 

       130        140        150        160        170        180 
QANLVIREAM ATDLILGANE QVLGVETYFG TCFAAKAVIL TTGTFLGGKI WIGGKSMAAG 

       190        200        210        220        230        240 
RAGEFAAVGL TETLNRLGFE TGRLKTGTPA RVDKRSVDYS RMEPQPPDDE VRWFSFDPEV 

       250        260        270        280        290        300 
WIEREQMNCH LTRTTAATHQ LIRDNLHLSP IYGGFIDSKG PRYCPSIEDK IVRFADKESH 

       310        320        330        340        350        360 
QIFIEPEGRD IPELYIQGFS TGLPENVQLA MLRTLPGLEN CVMLRAAYAV EYDYLPATQC 

       370        380        390        400        410        420 
YPTLMTKKIE GLFCAGQING TTGYEEAAAQ GLVAGINAAR FALGKELIVF PREESYLGTL 

       430        440        450        460        470        480 
VDDLCTKDLR EPYRMLTSRS EYRLVLRSDN ADQRLTPLGR EIGLIDNRRW QLFQSKQANI 

       490        500        510        520        530        540 
IAEKERLHET RIKERDQVAI AIVKDTEQKI KGSLSLADLL RRPSLHYLDL DRYGLGNPDI 

       550        560        570        580        590        600 
NLAEREGVEI EIKYSGYLKR QQNQIDQISR HSNRHLSPDI DYMKIETLSM ESREKLTKIK 

       610        620        630 
PATIGQASRI GGVNPADINA LLVYLEMRQM SAVKS 

« Hide

References

[1]"Complete genomic structure of the bloom-forming toxic cyanobacterium Microcystis aeruginosa NIES-843."
Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M., Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A., Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M. expand/collapse author list , Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.
DNA Res. 14:247-256(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NIES-843.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009552 Genomic DNA. Translation: BAG05320.1.
RefSeqYP_001660512.1. NC_010296.1.

3D structure databases

ProteinModelPortalB0JGQ4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING449447.MAE_54980.

Proteomic databases

PaxDbB0JGQ4.
PRIDEB0JGQ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG05320; BAG05320; MAE_54980.
GeneID5866340.
KEGGmar:MAE_54980.
PATRIC22635433. VBIMicAer59304_5016.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0445.
HOGENOMHOG000201060.
KOK03495.
OMAYINGLST.
OrthoDBEOG6W9X6J.
ProtClustDBPRK05192.

Enzyme and pathway databases

BioCycMAER449447:GHO8-5544-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_MICAN
AccessionPrimary (citable) accession number: B0JGQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 18, 2008
Last modified: February 19, 2014
This is version 39 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