P28720 (TGT_ZYMMO) 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:	ZMO0363

Organism

Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]

Taxonomic identifier

264203 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Zymomonas › Zymomonas mobilis › Zymomonas mobilis subsp. mobilis

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-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	Monomer.
Sequence similarities	Belongs to the queuine tRNA-ribosyltransferase family.
Sequence caution	The sequence AAA27704.1 differs from that shown. Reason: Erroneous initiation. The sequence AAA27705.1 differs from that shown. Reason: Erroneous initiation. The sequence AAG29862.1 differs from that shown. Reason: Erroneous initiation. 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	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

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 386

385

Queuine tRNA-ribosyltransferase HAMAP-Rule MF_00168

PRO_0000135563

Sites

Active site

102

1

Nucleophile

Metal binding

318

1

Zinc

Metal binding

320

1

Zinc

Metal binding

323

1

Zinc

Metal binding

349

1

Zinc

Binding site

103

1

Substrate

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

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

386

Helix Strand Turn

Details...

Beta strand

15 – 22

8

Beta strand

25 – 32

8

Beta strand

35 – 42

8

Beta strand

45 – 50

6

Helix

56 – 61

6

Beta strand

67 – 69

3

Helix

71 – 76

6

Turn

77 – 79

3

Helix

80 – 85

6

Helix

89 – 93

5

Beta strand

99 – 101

3

Helix

105 – 109

5

Helix

112 – 114

3

Beta strand

116 – 118

3

Beta strand

121 – 123

3

Turn

127 – 129

3

Beta strand

133 – 135

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

253 – 255

3

Beta strand

257 – 259

3

Helix

265 – 272

8

Turn

273 – 275

3

Beta strand

278 – 280

3

Helix

283 – 289

7

Beta strand

290 – 293

4

Beta strand

298 – 301

4

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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 12-386.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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: AAV88987.2.
Z11910 Genomic DNA. No translation available.

PIR

T46898.

RefSeq

YP_162098.2. NC_006526.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3EOS	X-ray	1.78	A	1-386	[»]
3EOU	X-ray	1.93	A	1-386	[»]
3GC4	X-ray	1.80	A	1-386	[»]
3GC5	X-ray	1.40	A	1-386	[»]
3GE7	X-ray	1.50	A	1-386	[»]
3GEV	X-ray	1.53	A	1-386	[»]
3HFY	X-ray	2.00	A	1-386	[»]
3RR4	X-ray	1.68	A	1-386	[»]
3S1G	X-ray	1.82	A	1-386	[»]
3SM0	X-ray	1.57	A	1-386	[»]
3TLL	X-ray	1.37	A	1-386	[»]
3UNT	X-ray	1.80	A	1-386	[»]
3UVI	X-ray	1.55	A	1-386	[»]
3V0Y	X-ray	1.64	A	1-386	[»]
4DXX	X-ray	1.66	A	1-386	[»]
4DY1	X-ray	2.04	A	1-386	[»]
4E2V	X-ray	1.18	A	1-386	[»]
4GCX	X-ray	1.42	A	1-386	[»]
4GD0	X-ray	1.29	A	1-386	[»]
4H6E	X-ray	1.42	A	1-386	[»]
4H7Z	X-ray	1.68	A	1-386	[»]
4HQV	X-ray	1.66	A	2-386	[»]
4HSH	X-ray	1.56	A	2-386	[»]
4HVX	X-ray	1.82	A	1-386	[»]

ProteinModelPortal

P28720.

SMR

P28720. Positions 11-386.

ModBase

Search...

Protein-protein interaction databases

STRING

264203.ZMO0363.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAV88987; AAV88987; ZMO0363.

GeneID

3188564.

KEGG

zmo:ZMO0363.

PATRIC

32566062. VBIZymMob102260_0345.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0343.

HOGENOM

HOG000223473.

KO

K00773.

ProtClustDB

PRK00112.

Enzyme and pathway databases

UniPathway

UPA00392.

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...

Other

BindingDB

P28720.

ChEMBL

CHEMBL2987.

EvolutionaryTrace

P28720.

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:	May 29, 2013
This is version 118 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program