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Q8KA85 (MNMG_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:CT2283
OrganismChlorobium tepidum
Taxonomic identifier1097 [NCBI]
Taxonomic lineageBacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 MF_00129

Cofactor

FAD.

Subunit structure

Homodimer. Heterotetramer of two MnmE and two MnmG subunits By similarity. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP MF_00129.

Sequence similarities

Belongs to the MnmG family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
NAD
   Technical term3D-structure
Complete proteome
Reference 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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 621621tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG HAMAP MF_00129
PRO_0000117086

Regions

Nucleotide binding8 – 136FAD HAMAP MF_00129
Nucleotide binding269 – 28315NAD Potential

Sites

Binding site1201FAD; via amide nitrogen and carbonyl oxygen
Binding site3661FAD

Secondary structure

1 ................................................................................................................... 621
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8KA85 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 752ED5CA7F9A38BF

FASTA62168,097
        10         20         30         40         50         60 
MYDVIVVGAG HAGCEAALAV ARGGLHCLLI TSDLSAVARM SCNPAIGGVA KGQITREIDA 

        70         80         90        100        110        120 
LGGEMGKAID ATGIQFRMLN RSKGPAMHSP RAQADKTQYS LYMRRIVEHE PNIDLLQDTV 

       130        140        150        160        170        180 
IGVSANSGKF SSVTVRSGRA IQAKAAILAC GTFLNGLIHI GMDHFPGGRS TAEPPVEGLT 

       190        200        210        220        230        240 
ESLASLGFSF GRLKTGTPPR IDSRSVDYTI VTEQPGDVDP VPFSFSSTSV ANRNLVSCYL 

       250        260        270        280        290        300 
TKTTEKTHDI LRTGFDRSPL FTGKVQGVGP RYCPSIEDKI SRFPDKSSHH IFLEPEGTDT 

       310        320        330        340        350        360 
VEMYVNGFST SLPEDIQIAG LRSIPGLEEA KMIRPGYAIE YDFFHPWQIR STMETRPVEN 

       370        380        390        400        410        420 
LFFAGQINGT SGYEEAAAQG LMAGINAVRK ILGKELIVLG RDQAYIGVLI DDLITKETKE 

       430        440        450        460        470        480 
PYRMFTSSAE HRLILRHDNA DLRLRKIGYD CNLVSSDDLH RTESIIKRVQ HCLEVMKTAK 

       490        500        510        520        530        540 
VTPAEINTLL MNKGLQELKT PARALSLIKR PGISLQDILE HSLSVRSAAE ELCNDPRVAE 

       550        560        570        580        590        600 
QVQIEIKYEG YIKREQLVAD RIARLDSLHI PDNFNYDSLN SLSSEGREKL LKHRPATIGQ 

       610        620 
ASRILGVSPS DVSILMIRLG R

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium."
Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. expand/collapse author list , Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed: 12093901] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49652 / DSM 12025 / TLS.
[2]"Crystal structures of the conserved tRNA-modifying enzyme GidA: implications for its interaction with MnmE and substrate."
Meyer S., Scrima A., Versees W., Wittinghofer A.
J. Mol. Biol. 380:532-547(2008) [PubMed: 18565343] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH FAD, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE006470 Genomic DNA. Translation: AAM73496.1.
RefSeqNP_663154.1. NC_002932.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3CP8X-ray3.20A/B/C/D1-621[»]
ProteinModelPortalQ8KA85.
SMRQ8KA85. Positions 1-619.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1007276.
GenomeReviewsGene locus CT2283 in contig AE006470_GR.
KEGGcte:CT2283.
NMPDRfig|194439.1.peg.2248.
PATRIC21402363. VBIChlTep116050_2076.
TIGRCT2283.

Phylogenomic databases

HOGENOMHBG284774.
OMAGFDRSPM.
ProtClustDBPRK05192.

Enzyme and pathway databases

BioCycCTEP194439:CT_2283-MONOMER.

Family and domain databases

HAMAPMF_00129. MnmG_GidA.
[Tree]
InterProIPR004416. GidA.
IPR002218. GIDA-rel.
IPR020595. GIDA-rel_CS.
[Graphical view]
KOK03495.
PfamPF01134. GIDA. 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_CHLTE
AccessionPrimary (citable) accession number: Q8KA85
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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