Reviewed, UniProtKB/Swiss-Prot P28720 (TGT_ZYMMO)

Names and origin

Protein names

Recommended name:
    Queuine tRNA-ribosyltransferase
    EC=2.4.2.29
Alternative name(s):
    tRNA-guanine transglycosylase
    Guanine insertion enzyme

Gene names

Name:	tgt
Ordered Locus Names:	ZMO0363

Organism

Zymomonas mobilis [Complete proteome] [HAMAP]

Taxonomic identifier

542 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Zymomonas

Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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). 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. HAMAP MF_00168
Pathway	tRNA modification; queuosine-tRNA biosynthesis. HAMAP MF_00168
Subunit structure	Monomer. HAMAP MF_00168
Sequence similarities	Belongs to the queuine tRNA-ribosyltransferase family.
Sequence caution	The sequence Z11910 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	Queuosine biosynthesis tRNA processing
Ligand	Metal-binding Zinc
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	queuosine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	queuine tRNA-ribosyltransferase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 386

385

Queuine tRNA-ribosyltransferase HAMAP MF_00168

PRO_0000135563

Sites

Active site

102

1

Nucleophile HAMAP MF_00168

Metal binding

318

1

Zinc HAMAP MF_00168

Metal binding

320

1

Zinc HAMAP MF_00168

Metal binding

323

1

Zinc HAMAP MF_00168

Metal binding

349

1

Zinc HAMAP MF_00168

Binding site

103

1

Substrate HAMAP MF_00168

Experimental info

Mutagenesis

103

1

S → A: Strongly reduces activity. Ref.6

Sequence conflict

312

1

T → K Ref.1

Sequence conflict

312

1

T → K Ref.2

Secondary structure

1

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386

Helix Strand Turn

Details...

Beta strand

15 – 22

8

Beta strand

25 – 32

8

Beta strand

35 – 43

9

Helix

56 – 61

6

Beta strand

67 – 70

4

Helix

71 – 76

6

Helix

80 – 85

6

Helix

89 – 93

5

Beta strand

99 – 102

4

Helix

105 – 108

4

Beta strand

116 – 118

3

Beta strand

121 – 123

3

Helix

137 – 147

11

Beta strand

150 – 153

4

Helix

165 – 187

23

Helix

190 – 195

6

Beta strand

197 – 202

6

Helix

208 – 221

14

Beta strand

224 – 228

5

Beta strand

232 – 235

4

Helix

237 – 247

11

Helix

248 – 250

3

Beta strand

257 – 259

3

Helix

265 – 272

8

Turn

273 – 275

3

Beta strand

278 – 280

3

Helix

283 – 289

7

Helix

305 – 307

3

Beta strand

314 – 317

4

Helix

321 – 325

5

Helix

328 – 336

9

Helix

340 – 366

27

Helix

370 – 381

12

Sequences

	Sequence		Length	Mass (Da)
	P28720-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 26754E08600BD941	FASTA	386	42,843
	10 20 30 40 50 60 MVEATAQETD RPRFSFSIAA REGKARTGTI EMKRGVIRTP AFMPVGTAAT VKALKPETVR 70 80 90 100 110 120 ATGADIILGN TYHLMLRPGA ERIAKLGGLH SFMGWDRPIL TDSGGYQVMS LSSLTKQSEE 130 140 150 160 170 180 GVTFKSHLDG SRHMLSPERS IEIQHLLGSD IVMAFDECTP YPATPSRAAS SMERSMRWAK 190 200 210 220 230 240 RSRDAFDSRK EQAENAALFG IQQGSVFENL RQQSADALAE IGFDGYAVGG LAVGEGQDEM 250 260 270 280 290 300 FRVLDFSVPM LPDDKPHYLM GVGKPDDIVG AVERGIDMFD CVLPTRSGRN GQAFTWDGPI 310 320 330 340 350 360 NIRNARFSED LTPLDSECHC AVCQKWSRAY IHHLIRAGEI LGAMLMTEHN IAFYQQLMQK 370 380 IRDSISEGRF SQFAQDFRAR YFARNS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis and overexpression of the Zymomonas mobilis tgt gene encoding tRNA-guanine transglycosylase: purification and biochemical characterization of the enzyme." Reuter K.K.H., Ficner R. J. Bacteriol. 177:5284-5288(1995) [PubMed: 7665516] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7, CHARACTERIZATION.
[2]	"Sequence analysis of 44B6 fosmid clone of Zymomonas mobilis ZM4." Ahn J.Y., Kang H.S. Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 31821 / ZM4 / CP4.
[3]	"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4." Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. , Kang H.L., Lee S.Y., Lee K.J., Kang H.S. Nat. Biotechnol. 23:63-68(2005) [PubMed: 15592456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31821 / ZM4 / CP4.
[4]	"Cloning and molecular characterization of the DNA ligase gene (lig) from Zymomonas mobilis." Shark K.B., Conway T. FEMS Microbiol. Lett. 75:19-26(1992) [PubMed: 1526462] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 31821 / ZM4 / CP4.
[5]	"Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange." Romier C., Reuter K., Suck D., Ficner R. EMBO J. 15:2850-2857(1996) [PubMed: 8654383] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[6]	"Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-guanine transglycosylase to elucidate the role of serine 103 for enzymatic activity." Graedler U., Ficner R., Garcia G.A., Stubbs M.T., Klebe G., Reuter K. FEBS Lett. 454:142-146(1999) [PubMed: 10413112] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-382, MUTAGENESIS OF SER-103.
[7]	"A new target for shigellosis: rational design and crystallographic studies of inhibitors of tRNA-guanine transglycosylase." Graedler U., Gerber H.-D., Goodenough-Lashua D.M., Garcia G.A., Ficner R., Reuter K., Stubbs M.T., Klebe G. J. Mol. Biol. 306:455-467(2001) [PubMed: 11178905] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
[8]	"De novo design, synthesis, and in vitro evaluation of inhibitors for prokaryotic tRNA-guanine transglycosylase: a dramatic sulfur effect on binding affinity." Meyer E.A., Brenk R., Castellano R.K., Furler M., Klebe G., Diederich F. ChemBioChem 3:250-253(2002) [PubMed: 11921407] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 12-386.
[9]	"Virtual screening for submicromolar leads of tRNA-guanine transglycosylase based on a new unexpected binding mode detected by crystal structure analysis." Brenk R., Naerum L., Graedler U., Gerber H.-D., Garcia G.A., Reuter K., Stubbs M.T., Klebe G. J. Med. Chem. 46:1133-1143(2003) [PubMed: 12646024] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 12-386.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L33777 Genomic DNA. Translation: AAA27704.1. Different initiation.
L33777 Genomic DNA. Translation: AAA27705.1. Different initiation.
AF313764 Genomic DNA. Translation: AAG29862.1. Different initiation.
AE008692 Genomic DNA. Translation: AAV88987.1. Different initiation.
Z11910 Genomic DNA. No translation available.

PIR

T46898.

RefSeq

YP_162098.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EFZ	X-ray	2.00	A	1-386	[»]
1ENU	X-ray	1.95	A	1-386	[»]
1F3E	X-ray	1.85	A	1-386	[»]
1K4G	X-ray	1.70	A	1-386	[»]
1K4H	X-ray	1.80	A	1-386	[»]
1N2V	X-ray	2.10	A	1-386	[»]
1OZM	X-ray	1.95	A	2-385	[»]
1OZQ	X-ray	1.90	A	2-385	[»]
1P0B	X-ray	1.70	A	2-385	[»]
1P0D	X-ray	1.90	A	2-385	[»]
1P0E	X-ray	2.40	A	2-385	[»]
1PUD	X-ray	1.85	A	1-386	[»]
1PXG	X-ray	1.70	A	2-382	[»]
1Q2R	X-ray	2.90	A/B/C/D	2-385	[»]
1Q2S	X-ray	3.20	A/B/C/D	2-385	[»]
1Q4W	X-ray	1.93	A	1-386	[»]
1Q63	X-ray	1.85	A	1-386	[»]
1Q65	X-ray	2.10	A	1-386	[»]
1Q66	X-ray	1.75	A	1-386	[»]
1R5Y	X-ray	1.20	A	2-385	[»]
1S38	X-ray	1.81	A	1-386	[»]
1S39	X-ray	1.95	A	1-386	[»]
1WKD	X-ray	2.60	A	2-385	[»]
1WKE	X-ray	2.20	A	2-385	[»]
1WKF	X-ray	2.20	A	2-385	[»]
1Y5V	X-ray	1.58	A	2-385	[»]
1Y5W	X-ray	1.58	A	2-385	[»]
1Y5X	X-ray	2.10	A/D	2-385	[»]
2BBF	X-ray	1.70	A	1-386	[»]
2NQZ	X-ray	1.46	A	2-386	[»]
2NSO	X-ray	1.60	A	1-386	[»]
2OKO	X-ray	1.50	A	2-386	[»]
2POT	X-ray	1.80	A	1-386	[»]
2PWU	X-ray	1.77	A	1-386	[»]
2PWV	X-ray	1.70	A	1-386	[»]
2QII	X-ray	1.70	A	1-386	[»]
2QZR	X-ray	1.95	A	2-386	[»]
2Z1V	X-ray	1.55	A	1-386	[»]
2Z1W	X-ray	1.63	A	1-386	[»]
2Z1X	X-ray	1.63	A	1-386	[»]
2Z7K	X-ray	1.28	A	1-386	[»]
3BL3	X-ray	2.25	A	1-386	[»]
3BLD	X-ray	1.19	A	1-386	[»]
3BLL	X-ray	1.26	A	1-386	[»]
3BLO	X-ray	1.60	A	1-386	[»]
3C2N	X-ray	1.58	A	1-386	[»]
3C2Y	X-ray	1.78	A	1-386	[»]
3C2Z	X-ray	1.65	A	1-386	[»]

ModBase

Search...

Genome annotation databases

GeneID

3188564.

GenomeReviews

Gene locus ZMO0363 in contig AE008692_GR.

KEGG

zmo:ZMO0363.

NMPDR

fig|264203.3.peg.859.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P28720.

Enzyme and pathway databases

BioCyc

ZMOB264203:ZMO0363-MON.

BRENDA

2.4.2.29. 1658.

Family and domain databases

HAMAP

MF_00168.
[Tree]

InterPro

IPR004803. QtRNA_ribo_trans.
IPR002616. tRNA_ribo_trans.
[Graphical view]

PANTHER

PTHR11962. tRNA_ribo_trans. 1 hit.

Pfam

PF01702. TGT. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00430. Q_tRNA_tgt. 1 hit.
TIGR00449. tgt_general. 1 hit.

ProtoNet

Search...

Entry information

Entry name

TGT_ZYMMO

Accession

Primary (citable) accession number: P28720
Secondary accession number(s): Q5NQL7, Q60247, Q9F5L7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 86 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)