Q5HUF2 (TGT_CAMJR) 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:	CJE1090

Organism

Campylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]

Taxonomic identifier

195099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	373 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 – 373	373	Queuine tRNA-ribosyltransferase HAMAP MF_00168		PRO_0000135460
Sites
	Active site	90	1	Nucleophile By similarity
	Metal binding	308	1	Zinc By similarity
	Metal binding	310	1	Zinc By similarity
	Metal binding	313	1	Zinc By similarity
	Metal binding	339	1	Zinc By similarity
	Binding site	91	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5HUF2 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 23197D2141F32B18	FASTA	373	42,554
	10 20 30 40 50 60 MEFKLKHKDG MARVCEITTA HSTFLTPVFM PVGTVGAVKS LDANDMKNEL DAKIILANTY 70 80 90 100 110 120 HMYLRPTSKV VKDFGGLHGF TKFDRSFLTD SGGFQAFSLS KNSKHFNEGI EFKSHIDGSR 130 140 150 160 170 180 HLFTPKSVLD AQYDFNSDIM MILDDLVALP ATKERVKISV DRTILWAKEA ITYHKNMQNK 190 200 210 220 230 240 GIGIGQNIFG IIQGGTDYEE RKRCALSLNE MPFDGLAIGG LSVGEENALM YETVQNLNPY 250 260 270 280 290 300 LDENRPRYLM GVGTPEDLVE NVERGVDMFD CVMPTRNARN GTFFTSFGKF NIKKAEFIND 310 320 330 340 350 360 HEVIDPTCSC YTCRNFSRGY LNHLFKAKEL TFFRLASLHN LHYYLELARK MREAILNNSF 370 TQFKRNFYHL RGK

References

[1]

"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species." Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. , Badger J.H., Fraser C.M., Nelson K.E. PLoS Biol. 3:72-85(2005) [PubMed: 15660156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RM1221.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000025 Genomic DNA. Translation: AAW35418.1.
RefSeq	YP_179083.1. NC_003912.7.
3D structure databases
ProteinModelPortal	Q5HUF2.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5HUF2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3231599.
GenomeReviews	Gene locus CJE1090 in contig CP000025_GR.
KEGG	cjr:CJE1090.
NMPDR	fig|195099.3.peg.1171.
PATRIC	20043989. VBICamJej134361_1114.
TIGR	CJE1090.
Phylogenomic databases
eggNOG	COG0343.
HOGENOM	HBG629929.
OMA	FMPVGTV.
ProtClustDB	PRK00112.
Enzyme and pathway databases
BioCyc	CJEJ195099:CJE_1090-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_CAMJR

Accession

Primary (citable) accession number: Q5HUF2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	February 15, 2005
Last modified:	January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program