O51749 (TGT_BORBU) 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:	BB_0809

Organism

Borrelia burgdorferi (Lyme disease spirochete)

Taxonomic identifier

139 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

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 Reference 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_0000135453
Sites
	Active site	90	1	Nucleophile By similarity
	Metal binding	305	1	Zinc By similarity
	Metal binding	307	1	Zinc By similarity
	Metal binding	310	1	Zinc By similarity
	Metal binding	336	1	Zinc By similarity
	Binding site	91	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O51749 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 7D7A554644439763	FASTA	375	43,199
	10 20 30 40 50 60 MFSVIKNDKH FNARVGFLNL PHGRVDIPCF MPVGTLGAMK GLKHAVLEKL ECNLMLANTY 70 80 90 100 110 120 HLYLRLGIKT VEKYVGLHNF TIWNKNFLTD SGGFRVFSFS DLRKIDLKGV HFKSHIDGSY 130 140 150 160 170 180 HYFTSEGIFA MQEIFGSDII MPLDICSSYG IDYNEANLYT NITTNWASST FKSSKNRKEG 190 200 210 220 230 240 YNGLLFLITQ GNFFKDLRKR SINDILELDS PGIAIGGISV GEPREKYLEI LEYSFLLIPK 250 260 270 280 290 300 EKPRYVMGIG TPHYILNAIY YGIDIFDCFN PARITRHGSL LTDNGIMCIG RKEYKDDTSK 310 320 330 340 350 360 VEKNCICTLC KRYSRGYLRH LIKSKELFGI VLASEHNIHY MFRLISKIRA AILNDDFLNF 370 RTSYLKKYEE ENFDE

References

[1]

"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C. Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000783 Genomic DNA. Translation: AAC67147.1.
PIR	H70200.
RefSeq	NP_212943.1. NC_001318.1.
3D structure databases
ProteinModelPortal	O51749.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBORT00000008789; EBBORP00000008119; EBBORG00000008788.
GeneID	1195667.
GenomeReviews	Gene locus BB_0809 in contig AE000783_GR.
KEGG	bbu:BB0809.
NMPDR	fig|224326.1.peg.1193.
PATRIC	20558283. VBIBorBur75917_1201.
TIGR	BB_0809.
Phylogenomic databases
GeneTree	EBGT00050000007233.
HOGENOM	HBG629929.
OMA	FMPVGTV.
ProtClustDB	PRK00112.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0809-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_BORBU

Accession

Primary (citable) accession number: O51749

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	June 1, 1998
Last modified:	January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program