Queuine tRNA-ribosyltransferase - Escherichia coli (strain K12)

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P0A847 (TGT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 74. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	b0406, JW0396

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Exchanges the guanine residue with 7-aminomethyl-7-deazaguanine in tRNAs with GU_N 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). 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.
Pathway	tRNA modification; tRNA-queuosine biosynthesis. HAMAP-Rule MF_00168
Subunit structure	Homotrimer or homodimer.
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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	queuosine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	metal 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 375

375

Queuine tRNA-ribosyltransferase HAMAP-Rule MF_00168

PRO_0000135471

Sites

Active site

Nucleophile

Metal binding

302

Zinc

Metal binding

304

Zinc

Metal binding

307

Zinc

Metal binding

333

Zinc By similarity

Binding site

Substrate

Experimental info

Mutagenesis

C → A: Slight loss of activity. Ref.10

Mutagenesis

S → A: Loss of activity. Ref.9 Ref.10

Mutagenesis

S → C: Loss of activity. Ref.9 Ref.10

Mutagenesis

S → F: Loss of activity. Ref.9 Ref.10

Mutagenesis

145

C → A: No loss of activity. Ref.10

Mutagenesis

232

C → A: Slight loss of activity. Ref.10

Mutagenesis

265

C → A: Significant loss of activity. Ref.10

Mutagenesis

302

C → A: Loss of activity. Ref.10

Mutagenesis

304

C → A: Loss of activity. Ref.10

Mutagenesis

307

C → A: Loss of activity. Ref.10

Mutagenesis

316

H → A: Slight loss of activity. Ref.10

Mutagenesis

317

H → A: Loss of activity. Ref.10

Mutagenesis

321

C → A: No loss of activity. Ref.10

Sequence conflict

54 – 55

IL → MV Ref.1

Sequence conflict

54 – 55

IL → MV Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P0A847 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 40271CA08D8A8820
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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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and organization of Escherichia coli genes involved in biosynthesis of the deazaguanine derivative queuine, a nutrient factor for eukaryotes." Reuter K., Slany R., Ullrich F., Kersten H. J. Bacteriol. 173:2256-2264(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"tRNA-guanine transglycosylase from Escherichia coli. Overexpression, purification and quaternary structure." Garcia G.A., Koch K.A., Chong S. J. Mol. Biol. 231:489-497(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9, CHARACTERIZATION.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The secD locus of E.coli codes for two membrane proteins required for protein export." Gardel C., Johnson K., Jacq A., Beckwith J. EMBO J. 9:3209-3216(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 141-375. Strain: K12.
[7]	Erratum Gardel C., Johnson K., Jacq A., Beckwith J. EMBO J. 9:4205-4206(1990) [PubMed] [Europe PMC] [Abstract]
[8]	"Genetic and molecular characterization of the Escherichia coli secD operon and its products." Pogliano K.J., Beckwith J. J. Bacteriol. 176:804-814(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 281-375.
[9]	"Serine 90 is required for enzymic activity by tRNA-guanine transglycosylase from Escherichia coli." Reuter K., Chong S., Ullrich F., Kersten H., Garcia G.A. Biochemistry 33:7041-7046(1994) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF SER-90.
[10]	"tRNA-guanine transglycosylase from Escherichia coli is a zinc metalloprotein. Site-directed mutagenesis studies to identify the zinc ligands." Chong S., Curnow A.W., Huston T.J., Garcia G.A. Biochemistry 34:3694-3701(1995) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ZINC LIGANDS.
[11]	"Cysteine 265 is in the active site of, but is not essential for catalysis by tRNA-guanine transglycosylase (TGT) from Escherichia coli." Garcia G.A., Chong S. J. Protein Chem. 16:11-17(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIVE SITE CYS-265.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M63939 Genomic DNA. Translation: AAA24667.1. U00096 Genomic DNA. Translation: AAC73509.1. AP009048 Genomic DNA. Translation: BAE76186.1. U82664 Genomic DNA. Translation: AAB40162.1. X56175 Genomic DNA. Translation: CAA39631.1. Sequence problems. X56175 Genomic DNA. Translation: CAA39632.1. Sequence problems. S68715 Genomic DNA. Translation: AAC60467.2.
PIR	C38530.
RefSeq	NP_414940.1. NC_000913.2. YP_488698.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0A847.
SMR	P0A847. Positions 3-364.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-36020N.
IntAct	P0A847. 39 interactions.
MINT	MINT-1219658.
STRING	511145.b0406.
Proteomic databases
PaxDb	P0A847.
PRIDE	P0A847.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73509; AAC73509; b0406. BAE76186; BAE76186; BAE76186.
GeneID	12934537. 949130.
KEGG	ecj:Y75_p0394. eco:b0406.
PATRIC	32115961. VBIEscCol129921_0422.
Organism-specific databases
EchoBASE	EB0989.
EcoGene	EG10996. tgt.
Phylogenomic databases
eggNOG	COG0343.
HOGENOM	HOG000223473.
KO	K00773.
OMA	MSPERSI.
ProtClustDB	PRK00112.
Enzyme and pathway databases
BioCyc	ECOL316407:JW0396-MONOMER.
SABIO-RK	P0A847.
UniPathway	UPA00392.
Gene expression databases
Genevestigator	P0A847.
Family and domain databases
Gene3D	3.20.20.105. 1 hit.
HAMAP	MF_00168. Q_tRNA_Tgt.
InterPro	IPR004803. Queuine_tRNA-ribosylTrfase. IPR002616. tRNA_ribo_trans-like. [Graphical view]
PANTHER	PTHR11962. PTHR11962. 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_ECOLI

Accession

Primary (citable) accession number: P0A847
Secondary accession number(s): P19675

Q47627

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	May 29, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents