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Reviewed, UniProtKB/Swiss-Prot O66962 (MNMG_AQUAE)

Last modified November 3, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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: aq_761
OrganismAquifex aeolicus [Complete proteome] [HAMAP]
Taxonomic identifier63363 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

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Protein attributes

Sequence length617 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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.

Cofactor

FAD. HAMAP MF_00129

Subunit structure

Homodimer. Heterotetramer of two mnmE and two mnmG subunits By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the mnmG family.

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Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
NAD
   Technical term3D-structure
Complete 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 functionFAD binding

Inferred from electronic annotation. Source: HAMAP

electron carrier activity

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 617617tRNA uridine 5-carboxymethylaminomethyl modification enzyme mnmG HAMAP MF_00129
PRO_0000117046

Regions

Nucleotide binding14 – 196FAD HAMAP MF_00129
Nucleotide binding280 – 29415NAD Potential

Sites

Binding site1261FAD; via amide nitrogen and carbonyl oxygen HAMAP MF_00129
Binding site1811FAD HAMAP MF_00129
Binding site3771FAD HAMAP MF_00129

Secondary structure

1 .................................................................................................. 617
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O66962-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 1DAB1BDFEFCBA6DD

FASTA61769,644
        10         20         30         40         50         60 
MAWVVDEFDV VVIGGGHAGI EAALAAARMG AKTAMFVLNA DTIGQMSCNP AIGGIAKGIV 

        70         80         90        100        110        120 
VREIDALGGE MGKAIDQTGI QFKMLNTRKG KAVQSPRAQA DKKRYREYMK KVCENQENLY 

       130        140        150        160        170        180 
IKQEEVVDII VKNNQVVGVR TNLGVEYKTK AVVVTTGTFL NGVIYIGDKM IPGGRLGEPR 

       190        200        210        220        230        240 
SEGLSDFYRR FDFPLIRFKT GTPARLDKRT IDFSALEVAP GDDPPPKFSF WTEPVGSYWF 

       250        260        270        280        290        300 
PKGKEQVNCW ITYTTPKTHE IIRKNLHRTA LYGGLIKGIG PRYCPSIEDK IVKFPDKERH 

       310        320        330        340        350        360 
QIFLEPEGLD TIEIYPNGLS TSLPEEVQWE MYRSIPGLEN VVLIRPAYAI EYDVVPPTEL 

       370        380        390        400        410        420 
YPTLETKKIR GLFHAGNFNG TTGYEEAAGQ GIVAGINAAL RAFGKEPIYL RRDESYIGVM 

       430        440        450        460        470        480 
IDDLTTKGVT EPYRLFTSRS EYRLYIRQDN AILRLAKLGR ELGLLSEEQY KLVKELEREI 

       490        500        510        520        530        540 
EKWKEFYKSE RVSVAVGGDT RSYSVATLMT MNYTLDDVKE KFGYEVPQHP YVKEEVEIQL 

       550        560        570        580        590        600 
KYEPYIERER KLNEKLKKLE DTKIPPDIDY DKIPGLTKEA REKLKKFKPI TVGQASRIDG 

       610 
ITPAAITALL VYLGKLD

« Hide

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References

« Hide 'large scale' references
[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
[2]"Crystal structure of gidA from Aquifex aeolicus."
RIKEN structural genomics initiative (RSGI)
Submitted (JAN-2008) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH FAD, SUBUNIT.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AE000657 Genomic DNA. Translation: AAC06917.1.
PIRG70366.
RefSeqNP_213523.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2ZXHX-ray3.20A/B1-617[»]
2ZXIX-ray2.30A/B/C/D1-617[»]
ModBaseSearch...

Genome annotation databases

GeneID1193412.
GenomeReviewsGene locus aq_761 in contig AE000657_GR.
KEGGaae:aq_761.
NMPDRfig|224324.1.peg.538.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO66962.
OMAGPAVWAL.

Enzyme and pathway databases

BioCycAAEO224324:AQ_761-MON.

Family and domain databases

HAMAPMF_00129.
[Tree]
InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004416. GidA.
IPR002218. GIDA-rel.
IPR020595. GIDA-rel_CS.
[Graphical view]
PANTHERPTHR11806. GIDA. 1 hit.
PfamPF01134. GIDA. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
ProDomPD003738. GIDA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00136. gidA. 1 hit.
PROSITEPS01280. GIDA_1. 1 hit.
PS01281. GIDA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameMNMG_AQUAE
AccessionPrimary (citable) accession number: O66962
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: November 3, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents