Q8DLI5 (SYE_THEEB) 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:	tll0506

Organism

Thermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]

Taxonomic identifier

197221 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Thermosynechococcus › Thermosynechococcus elongatus

Protein attributes

Sequence length	485 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Non-discriminating glutamyl-tRNA synthetase. 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). Acylates both tRNA(Glu) and tRNA(Gln) with glutamate, but has 13-fold higher efficiency with tRNA(Glu). Ref.2
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022_B
Cofactor	Does not require zinc. Ref.2
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm HAMAP-Rule MF_00022_B.
Miscellaneous	This organism lacks a tRNA synthetase for tRNA(Gln). Instead, tRNA(Gln) is first charged with Glu, and then the bound glutamate is converted to glutamine by GatCAB. HAMAP-Rule MF_00022_B
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.
Biophysicochemical properties	Kinetic parameters: KM=0.79 µM for tRNA-Glu Ref.2 KM=3.7 µM for tRNA-Gln

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: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP glutamate-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 485

485

Glutamate--tRNA ligase HAMAP-Rule MF_00022_B

PRO_0000119674

Regions

Region

210 – 214

5

Glutamate binding HAMAP-Rule MF_00022_B

Motif

9 – 19

11

"HIGH" region HAMAP-Rule MF_00022_B

Motif

248 – 252

5

"KMSKS" region HAMAP-Rule MF_00022_B

Sites

Binding site

6

1

Glutamate

Binding site

192

1

Glutamate

Binding site

251

1

ATP By similarity

Secondary structure

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485

Helix Strand Turn

Details...

Beta strand

4 – 7

4

Helix

17 – 32

16

Beta strand

36 – 41

6

Beta strand

45 – 48

4

Helix

51 – 63

13

Beta strand

69 – 74

6

Helix

75 – 77

3

Helix

79 – 91

13

Beta strand

94 – 98

5

Helix

102 – 115

14

Turn

124 – 127

4

Helix

130 – 138

9

Beta strand

144 – 147

4

Beta strand

154 – 159

6

Turn

160 – 162

3

Beta strand

163 – 168

6

Helix

169 – 172

4

Beta strand

174 – 179

6

Helix

192 – 202

11

Beta strand

206 – 211

6

Helix

212 – 216

5

Helix

217 – 227

11

Beta strand

234 – 238

5

Beta strand

244 – 248

5

Helix

258 – 263

6

Helix

268 – 277

10

Turn

284 – 286

3

Helix

292 – 298

7

Helix

313 – 324

12

Helix

329 – 342

14

Turn

349 – 352

4

Helix

353 – 363

11

Helix

364 – 366

3

Helix

370 – 372

3

Helix

373 – 381

9

Beta strand

382 – 384

3

Helix

389 – 395

7

Helix

400 – 410

11

Beta strand

413 – 415

3

Helix

419 – 433

15

Helix

437 – 449

13

Beta strand

450 – 453

4

Helix

457 – 466

10

Helix

470 – 484

15

Sequences

	Sequence		Length	Mass (Da)
	Q8DLI5 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: C3547C6415FDDCBA	FASTA	485	54,362
	10 20 30 40 50 60 MTVRVRLAPS PTGNLHIGTA RTAVFNWLYA RHRGGKFILR IEDTDRERSR PEYTENILEG 70 80 90 100 110 120 LQWLGLTWDE GPYFQSDRLD LYRQAIQTLL DKGLAYYCYC TPEELEALRA EQKAKGQAPR 130 140 150 160 170 180 YDNRHRHLTP EEQAAFEAAG RTPVIRFKIE DDRQIEWQDL VRGRVSWQGA DLGGDMVIAR 190 200 210 220 230 240 AAPRGEIGYP LYNLVVVVDD IAMGITDVIR GEDHIGNTPK QILLYEALGA TPPNFAHTPL 250 260 270 280 290 300 ILNSTGQKLS KRDGVTSISD FRAMGYLAPA LANYMTLLGW SPPEGVGELF TLDLAAKHFS 310 320 330 340 350 360 FERINKAGAR FDWDKLNWLN RQYIQQLEPE EFLAELIPLW QGAGYAFDEE RDRPWLFDLA 370 380 390 400 410 420 QLLQPGLNTL REAIDQGAVF FIPSVTFDSE AMAQLGQPQS ATILAYLLEH LPAEPALTVA 430 440 450 460 470 480 MGQQLIQQAA KAAGVKKGAT MRTLRAALTG AVHGPDLMAA WQILHQRGWD EPRLAAALKQ AQTTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1." Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. , Takeuchi C., Yamada M., Tabata S. DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BP-1.
[2]	"Crystal structure of a non-discriminating glutamyl-tRNA synthetase." Schulze J.O., Masoumi A., Nickel D., Jahn M., Jahn D., Schubert W.-D., Heinz D.W. J. Mol. Biol. 361:888-897(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH GLUTAMATE, FUNCTION, ABSENCE OF COFACTOR REQUIREMENT, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000039 Genomic DNA. Translation: BAC08058.1.

RefSeq

NP_681296.1. NC_004113.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CFO	X-ray	2.45	A/B	2-485	[»]

ProteinModelPortal

Q8DLI5.

SMR

Q8DLI5. Positions 2-485.

ModBase

Search...

Protein-protein interaction databases

STRING

197221.tll0506.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAC08058; BAC08058; BAC08058.

GeneID

1012165.

KEGG

tel:tll0506.

PATRIC

23926260. VBITheElo119873_0533.

Phylogenomic databases

eggNOG

COG0008.

HOGENOM

HOG000252722.

KO

K01885.

OMA

HGATSIA.

ProtClustDB

PRK01406.

Family and domain databases

Gene3D

1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.

HAMAP

MF_00022_B. Glu_tRNA_synth_B.

InterPro

IPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_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]

PANTHER

PTHR10119. PTHR10119. 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...

Other

EvolutionaryTrace

Q8DLI5.

Entry information

Entry name

SYE_THEEB

Accession

Primary (citable) accession number: Q8DLI5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program