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C4ZAW9 (C4ZAW9_EUBR3) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Queuine tRNA-ribosyltransferase HAMAP-Rule MF_00168 RuleBase RU003777
EC=2.4.2.29 HAMAP-Rule MF_00168 RuleBase RU003777
Alternative name(s):
Guanine insertion enzyme HAMAP-Rule MF_00168
tRNA-guanine transglycosylase HAMAP-Rule MF_00168
Gene names
Name:tgt HAMAP-Rule MF_00168
Ordered Locus Names:EUBREC_1880
OrganismEubacterium rectale (strain ATCC 33656 / VPI 0990) [Complete proteome] [HAMAP]
Taxonomic identifier515619 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Eubacteriaceae › Eubacterium ›

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Exchanges the guanine residue with 7-aminomethyl-7-deazaguanine in tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr). After this exchange, a cyclopentendiol moiety is attached to the 7-aminomethyl group of 7-deazaguanine, resulting in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) By similarity. HAMAP-Rule MF_00168 RuleBase RU003777 SAAS SAAS004803

Catalytic activity

Guanine34 in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine34 in tRNA + guanine. HAMAP-Rule MF_00168 SAAS SAAS004803

Guanine34 in tRNA + queuine = queuosine34 in tRNA + guanine. HAMAP-Rule MF_00168 SAAS SAAS004803

[tRNA]-guanine + queuine = [tRNA]-queuine + guanine. RuleBase RU003777

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00168 RuleBase RU003777 SAAS SAAS004803

Pathway

tRNA modification; tRNA-queuosine biosynthesis. HAMAP-Rule MF_00168 SAAS SAAS004803

Sequence similarities

Belongs to the queuine tRNA-ribosyltransferase family. HAMAP-Rule MF_00168 RuleBase RU003777

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site911Nucleophile By similarity HAMAP-Rule MF_00168
Metal binding3111Zinc By similarity HAMAP-Rule MF_00168
Metal binding3131Zinc By similarity HAMAP-Rule MF_00168
Metal binding3161Zinc By similarity HAMAP-Rule MF_00168
Metal binding3421Zinc By similarity HAMAP-Rule MF_00168
Binding site921Substrate By similarity HAMAP-Rule MF_00168

Sequences

Sequence LengthMass (Da)Tools
C4ZAW9 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: E27419B5096E8FAD

FASTA38042,999
        10         20         30         40         50         60 
MAKYELLKQE GRAKRGTFHT VHGDIQTPVF MNVGTVGAIK GAVSTDDLKE IKCQVELSNT 

        70         80         90        100        110        120 
YHLHVRTGDK IIKELGGLHK FMVWDRPILT DSGGFQVFSL AGLRKIKEEG VYFNSHIDGA 

       130        140        150        160        170        180 
KIFMGPEESM QIQSNLGSTI AMAFDECPSS VADRQYVTNS VNRTARWLER CKKEMARLNS 

       190        200        210        220        230        240 
LPDTINKEQL LFGINQGAIY DDIRIDHAKR ISELELDGYA VGGLAVGESH EEMYHILDET 

       250        260        270        280        290        300 
VPHLPVNKPT YLMGVGTPAN ILEGVERGID FFDCVYPSRN GRHGHVYTNH GKLNLFNQKY 

       310        320        330        340        350        360 
QKDMRPIEEG CNCPACRTYS RAYIRHLLKA KEMLGMRLCV LHNLYFYNNM MEEIRDSLDA 

       370        380 
GRFASYKAEK LYGMTQGEQS

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References

[1]"Characterizing a model human gut microbiota composed of members of its two dominant bacterial phyla."
Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., Hettich R.L., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33656 / VPI 0990.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001107 Genomic DNA. Translation: ACR75624.1.
RefSeqYP_002937758.1. NC_012781.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING515619.EUBREC_1880.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR75624; ACR75624; EUBREC_1880.
GeneID7964075.
KEGGere:EUBREC_1880.
PATRIC21871953. VBIEubRec107985_1625.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0343.
HOGENOMHOG000223473.
KOK00773.
OMAMSPERSI.
ProtClustDBPRK00112.

Enzyme and pathway databases

BioCycEREC515619:GHMX-1887-MONOMER.
UniPathwayUPA00392.

Family and domain databases

Gene3D3.20.20.105. 1 hit.
HAMAPMF_00168. Q_tRNA_Tgt.
InterProIPR004803. Queuine_tRNA-ribosylTrfase.
IPR002616. tRNA_ribo_trans.
[Graphical view]
PANTHERPTHR11962. PTHR11962. 1 hit.
PfamPF01702. TGT. 1 hit.
[Graphical view]
SUPFAMSSF51713. tRNA_ribo_trans. 1 hit.
TIGRFAMsTIGR00430. Q_tRNA_tgt. 1 hit.
TIGR00449. tgt_general. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC4ZAW9_EUBR3
AccessionPrimary (citable) accession number: C4ZAW9
Entry history
Integrated into UniProtKB/TrEMBL: July 28, 2009
Last sequence update: July 28, 2009
Last modified: May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info