Q1RFD5 (TGT_ECOUT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	UTI89_C0428

Organism

Escherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

364106 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Protein existence	Inferred 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 MF_00168
Catalytic activity	[tRNA]-guanine + queuine = [tRNA]-queuine + guanine. HAMAP MF_00168 [tRNA]-guanine + 7-aminomethyl-7-carbaguanine = [tRNA]-7-aminomethyl-7-carbaguanine + guanine. HAMAP MF_00168
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00168
Pathway	tRNA modification; tRNA-queuosine biosynthesis. HAMAP MF_00168
Sequence similarities	Belongs to the queuine tRNA-ribosyltransferase family.

Ontologies

Keywords
Biological process	Queuosine biosynthesis tRNA processing
Ligand	Metal-binding Zinc
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	queuosine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW queuine tRNA-ribosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 375	375	Queuine tRNA-ribosyltransferase HAMAP MF_00168		PRO_1000016789
Sites
	Active site	89	1	Nucleophile By similarity
	Metal binding	302	1	Zinc By similarity
	Metal binding	304	1	Zinc By similarity
	Metal binding	307	1	Zinc By similarity
	Metal binding	333	1	Zinc By similarity
	Binding site	90	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1RFD5 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: 40271CA08D8A8820	FASTA	375	42,594
	10 20 30 40 50 60 MKFELDTTDG RARRGRLVFD RGVVETPCFM PVGTYGTVKG MTPEEVEATG AQIILGNTFH 70 80 90 100 110 120 LWLRPGQEIM KLHGDLHDFM QWKGPILTDS GGFQVFSLGD IRKITEQGVH FRNPINGDPI 130 140 150 160 170 180 FLDPEKSMEI QYDLGSDIVM IFDECTPYPA DWDYAKRSME MSLRWAKRSR ERFDSLGNKN 190 200 210 220 230 240 ALFGIIQGSV YEDLRDISVK GLVDIGFDGY AVGGLAVGEP KADMHRILEH VCPQIPADKP 250 260 270 280 290 300 RYLMGVGKPE DLVEGVRRGI DMFDCVMPTR NARNGHLFVT DGVVKIRNAK YKSDTGPLDP 310 320 330 340 350 360 ECDCYTCRNY SRAYLHHLDR CNEILGARLN TIHNLRYYQR LMAGLRKAIE EGKLESFVTD 370 FYQRQGREVP PLNVD

References

[1]

"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach." Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UTI89 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000243 Genomic DNA. Translation: ABE05929.1.
RefSeq	YP_539460.1. NC_007946.1.
3D structure databases
ProteinModelPortal	Q1RFD5.
SMR	Q1RFD5. Positions 1-368.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1RFD5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000069332; EBESCP00000066810; EBESCG00000068379.
GeneID	3993726.
GenomeReviews	Gene locus UTI89_C0428 in contig CP000243_GR.
KEGG	eci:UTI89_C0428.
PATRIC	18450527. VBIEscCol42261_0535.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0343.
GeneTree	EBGT00050000010492.
HOGENOM	HBG629929.
OMA	FMPVGTV.
ProtClustDB	PRK00112.
Enzyme and pathway databases
BioCyc	ECOL364106:UTI89_C0428-MONOMER.
Family and domain databases
HAMAP	MF_00168. Q_tRNA_Tgt. [Tree]
InterPro	IPR004803. Queuine_tRNA-ribosylTrfase. IPR002616. tRNA_ribo_trans. [Graphical view]
Gene3D	G3DSA:3.20.20.105. tRNA_ribo_trans. 1 hit.
KO	K00773.
PANTHER	PTHR11962. tRNA_ribo_trans. 1 hit.
Pfam	PF01702. TGT. 1 hit. [Graphical view]
SUPFAM	SSF51713. tRNA_ribo_trans. 1 hit.
TIGRFAMs	TIGR00430. Q_tRNA_tgt. 1 hit. TIGR00449. Tgt_general. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TGT_ECOUT

Accession

Primary (citable) accession number: Q1RFD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 16, 2006
Last modified:	January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program