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Q7NYC7 (TGT_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 70. 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:
Queuine tRNA-ribosyltransferase
EC=2.4.2.29
Alternative name(s):
Guanine insertion enzyme
tRNA-guanine transglycosylase
Gene names
Name:tgt
Ordered Locus Names:CV_1347
OrganismChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757) [Complete proteome] [HAMAP]
Taxonomic identifier243365 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium ›

Protein attributes

Sequence length371 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

Catalytic activity

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

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

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00168

Pathway

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

Sequence similarities

Belongs to the queuine tRNA-ribosyltransferase family.

Ontologies

Keywords
   Biological processQueuosine biosynthesis
tRNA processing
   LigandMetal-binding
Zinc
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processqueuosine biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

queuine tRNA-ribosyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 371371Queuine tRNA-ribosyltransferase HAMAP-Rule MF_00168
PRO_1000016777

Sites

Active site901Nucleophile By similarity
Metal binding3031Zinc By similarity
Metal binding3051Zinc By similarity
Metal binding3081Zinc By similarity
Metal binding3341Zinc By similarity
Binding site911Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NYC7 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 9A18555AD357A5E9

FASTA37141,937
        10         20         30         40         50         60 
MLKFTVHKTS GGARRGTLEL NHGTVETPVF QPVGTYGSVK AMSPVELNDI GAQIILGNTF 

        70         80         90        100        110        120 
HLWLRPGLEI VEQFGGLHEF IGWDKPILTD SGGFQVFSLS DMRKLTEEGC TFQSPINGDK 

       130        140        150        160        170        180 
LFLSPEISMK IQTVLNSDIV MQLDECTPGQ VDHATAQKSL QMSLRWAERS RRAFDDLKNP 

       190        200        210        220        230        240 
NALFGIVQGN LYTDLRQESL EGLMQVGFDG IAIGGLSVGE PKPEMYRMLT ELKDMLPADK 

       250        260        270        280        290        300 
PHYLMGVGTP EDLVHGVANG VDMFDCVMPT RNARNGWIFT QWGDVKIKNA RYKDDKKPLD 

       310        320        330        340        350        360 
EECACYACRN FSRAYLHHLH RVGEILGARL NTIHNLFYYQ ELMREMRKAI EEDRFEDFRL 

       370 
EFAAKRARSV N

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016825 Genomic DNA. Translation: AAQ59022.1.
RefSeqNP_901017.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NYC7.
SMRQ7NYC7. Positions 2-365.
ModBaseSearch...

Protein-protein interaction databases

STRING243365.CV_1347.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ59022; AAQ59022; CV_1347.
GeneID2548605.
KEGGcvi:CV_1347.
PATRIC21437494. VBIChrVio67196_1321.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0343.
HOGENOMHOG000223473.
KOK00773.
OMAMSPERSI.
ProtClustDBPRK00112.

Enzyme and pathway databases

BioCycCVIO243365:GHUD-1385-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-like.
[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 nameTGT_CHRVO
AccessionPrimary (citable) accession number: Q7NYC7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 15, 2003
Last modified: May 29, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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