P27000 (SYE_THET8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS

Gene names

Name:	gltX
Ordered Locus Names:	TTHA0438

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). Ref.4 Ref.6
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B
Enzyme regulation	In the absence of bound tRNA, ATP is bound in a non-productive mode, and the enzyme cannot activate amino acids. Ref.6
Subunit structure	Monomer.
Subcellular location	Cytoplasm HAMAP MF_00022_B.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.
Biophysicochemical properties	Kinetic parameters: KM=4.7 µM for tRNA-Glu Ref.4

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate-tRNA ligase 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 – 468

468

Glutamate--tRNA ligase HAMAP MF_00022_B

PRO_0000119683

Regions

Nucleotide binding

243 – 247

5

ATP HAMAP MF_00022_B

Region

5 – 7

3

Glutamate binding HAMAP MF_00022_B

Region

187 – 191

5

Glutamate binding HAMAP MF_00022_B

Region

432 – 447

16

Interaction with tRNA HAMAP MF_00022_B

Motif

8 – 18

11

"HIGH" region HAMAP MF_00022_B

Motif

243 – 247

5

"KMSKS" region HAMAP MF_00022_B

Sites

Binding site

15

1

ATP

Binding site

41

1

Glutamate

Binding site

205

1

Glutamate

Binding site

208

1

ATP

Binding site

236

1

ATP; via amide nitrogen and carbonyl oxygen

Site

354

1

Interaction with tRNA; via carbonyl oxygen

Site

358

1

Essential for discrimination between tRNA(Glu) and tRNA(Gln)

Experimental info

Mutagenesis

358

1

R → Q: Reduces affinity for tRNA and abolishes the ability to discriminate between tRNA(Glu) and tRNA(Gln). Ref.4

Sequence conflict

74 – 77

4

GGPH → AAPT in CAA45854. Ref.1

Secondary structure

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468

Helix Strand Turn

Details...

Beta strand

3 – 6

4

Beta strand

11 – 13

3

Helix

16 – 31

16

Beta strand

35 – 38

4

Turn

45 – 47

3

Helix

52 – 62

11

Beta strand

71 – 73

3

Beta strand

76 – 78

3

Helix

82 – 85

4

Helix

86 – 97

12

Turn

98 – 100

3

Beta strand

101 – 105

5

Helix

109 – 118

10

Beta strand

119 – 121

3

Helix

125 – 128

4

Helix

131 – 139

9

Beta strand

145 – 148

4

Beta strand

155 – 160

6

Turn

161 – 163

3

Beta strand

164 – 169

6

Helix

170 – 172

3

Beta strand

177 – 179

3

Helix

187 – 197

11

Beta strand

202 – 206

5

Helix

207 – 209

3

Turn

210 – 212

3

Helix

213 – 222

10

Beta strand

229 – 233

5

Beta strand

241 – 243

3

Turn

246 – 248

3

Helix

253 – 258

6

Helix

263 – 272

10

Helix

286 – 292

7

Helix

295 – 297

3

Helix

307 – 320

14

Helix

324 – 337

14

Helix

345 – 355

11

Helix

356 – 358

3

Helix

364 – 368

5

Helix

370 – 372

3

Helix

381 – 395

15

Helix

398 – 403

6

Helix

409 – 422

14

Helix

428 – 438

11

Helix

447 – 454

8

Helix

456 – 467

12

Sequences

	Sequence		Length	Mass (Da)
	P27000 [UniParc]. Last modified March 29, 2005. Version 2. Checksum: 920E7F3363AF19E9	FASTA	468	53,910
	10 20 30 40 50 60 MVVTRIAPSP TGDPHVGTAY IALFNYAWAR RNGGRFIVRI EDTDRARYVP GAEERILAAL 70 80 90 100 110 120 KWLGLSYDEG PDVGGPHGPY RQSERLPLYQ KYAEELLKRG WAYRAFETPE ELEQIRKEKG 130 140 150 160 170 180 GYDGRARNIP PEEAEERARR GEPHVIRLKV PRPGTTEVKD ELRGVVVYDN QEIPDVVLLK 190 200 210 220 230 240 SDGYPTYHLA NVVDDHLMGV TDVIRAEEWL VSTPIHVLLY RAFGWEAPRF YHMPLLRNPD 250 260 270 280 290 300 KTKISKRKSH TSLDWYKAEG FLPEALRNYL CLMGFSMPDG REIFTLEEFI QAFTWERVSL 310 320 330 340 350 360 GGPVFDLEKL RWMNGKYIRE VLSLEEVAER VKPFLREAGL SWESEAYLRR AVELMRPRFD 370 380 390 400 410 420 TLKEFPEKAR YLFTEDYPVS EKAQRKLEEG LPLLKELYPR LRAQEEWTEA ALEALLRGFA 430 440 450 460 AEKGVKLGQV AQPLRAALTG SLETPGLFEI LALLGKERAL RRLERALA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Glutamyl-tRNA synthetase from Thermus thermophilus HB8. Molecular cloning of the gltX gene and crystallization of the overproduced protein." Nureki O., Suzuki K., Hara-Yokoyama M., Kohno T., Matsuzawa H., Ohta T., Shimizu T., Morikawa K., Miyazawa T., Yokoyama S. Eur. J. Biochem. 204:465-472(1992) [PubMed: 1541262] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB8 / ATCC 27634 / DSM 579.
[3]	"Architectures of class-defining and specific domains of glutamyl-tRNA synthetase." Nureki O., Vassylyev D.G., Katayanagi K., Shimizu T., Sekine S., Kigawa T., Miyazawa T., Yokoyama S., Morikawa K. Science 267:1958-1965(1995) [PubMed: 7701318] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[4]	"Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase." Sekine S., Nureki O., Shimada A., Vassylyev D.G., Yokoyama S. Nat. Struct. Biol. 8:203-206(2001) [PubMed: 11224561] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH TRNA-GLU, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-358.
[5]	"ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding." Sekine S., Nureki O., Dubois D.Y., Bernier S., Chenevert R., Lapointe J., Vassylyev D.G., Yokoyama S. EMBO J. 22:676-688(2003) [PubMed: 12554668] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ATP; GLUTAMATE AND TRNA.
[6]	"Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase." Sekine S., Shichiri M., Bernier S., Chenevert R., Lapointe J., Yokoyama S. Structure 14:1791-1799(2006) [PubMed: 17161369] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH ATP; GLUTAMATE AND TRNA, FUNCTION, ENZYME REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X64557 Genomic DNA. Translation: CAA45854.1.
AP008226 Genomic DNA. Translation: BAD70261.1.

RefSeq

YP_143704.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G59	X-ray	2.40	A/C	1-468	[»]
1GLN	X-ray	2.50	A	1-468	[»]
1J09	X-ray	1.80	A	1-468	[»]
1N75	X-ray	1.90	A	1-468	[»]
1N77	X-ray	2.40	A/B	1-468	[»]
1N78	X-ray	2.10	A/B	1-468	[»]
2CUZ	X-ray	1.98	A	1-468	[»]
2CV0	X-ray	2.40	A/B	1-468	[»]
2CV1	X-ray	2.41	A/B	1-468	[»]
2CV2	X-ray	2.69	A/B	1-468	[»]
2DXI	X-ray	2.20	A/B	1-468	[»]

ProteinModelPortal

P27000.

SMR

P27000. Positions 1-468.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29168N.

STRING

P27000.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3168748.

GenomeReviews

Gene locus TTHA0438 in contig AP008226_GR.

KEGG

ttj:TTHA0438.

NMPDR

fig|300852.3.peg.504.

PATRIC

23955847. VBITheThe93045_0438.

Phylogenomic databases

eggNOG

COG0008.

HOGENOM

HBG628189.

OMA

MAHIPLI.

PhylomeDB

P27000.

ProtClustDB

PRK01406.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA0438-MONOMER.

Family and domain databases

HAMAP

MF_00022_B. Glu_tRNA_synth_B.
[Tree]

InterPro

IPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

Gene3D

G3DSA:1.10.8.70. aa-tRNA-synth_I_codon-bd_sub1. 1 hit.
G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.

KO

K01885.

PANTHER

PTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.

Pfam

PF00749. tRNA-synt_1c. 1 hit.
[Graphical view]

PRINTS

PR00987. TRNASYNTHGLU.

SUPFAM

SSF48163. tRNA-synt_bind. 1 hit.

TIGRFAMs

TIGR00464. GltX_bact. 1 hit.

PROSITE

PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SYE_THET8

Accession

Primary (citable) accession number: P27000
Secondary accession number(s): Q5SL55

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	March 29, 2005
Last modified:	January 25, 2012
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program