Reviewed, UniProtKB/Swiss-Prot P00962 (SYQ_ECOLI)

Names and origin

Protein names

Recommended name:
    Glutaminyl-tRNA synthetase
    EC=6.1.1.18
Alternative name(s):
    Glutamine--tRNA ligase
      Short name=GlnRS

Gene names

Name:	glnS
Ordered Locus Names:	b0680, JW0666

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	554 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)

Catalytic activity	ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln).
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

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 Direct protein sequencing
Gene Ontology (GO)
Biological process	glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP glutamine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 554

553

Glutaminyl-tRNA synthetase

Regions

Motif

34 – 44

11

"HIGH" region

Motif

268 – 272

5

"KMSKS" region

Sites

Binding site

271

1

ATP By similarity

Experimental info

Sequence conflict

549 – 554

6

WAKVGE → GRK Ref.2

Secondary structure

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554

Helix Strand Turn

Details...

Helix

11 – 21

11

Beta strand

29 – 32

4

Helix

42 – 57

16

Beta strand

61 – 66

6

Helix

71 – 73

3

Helix

76 – 88

13

Beta strand

94 – 96

3

Helix

100 – 103

4

Helix

104 – 116

13

Beta strand

119 – 123

5

Helix

127 – 134

8

Beta strand

137 – 139

3

Turn

145 – 148

4

Helix

151 – 162

12

Beta strand

172 – 175

4

Helix

184 – 186

3

Beta strand

190 – 194

5

Turn

200 – 202

3

Beta strand

207 – 210

4

Helix

212 – 222

11

Beta strand

226 – 231

6

Helix

232 – 234

3

Turn

235 – 237

3

Helix

238 – 246

9

Beta strand

255 – 259

5

Helix

271 – 279

9

Beta strand

282 – 284

3

Helix

294 – 300

7

Helix

304 – 314

11

Helix

325 – 339

15

Beta strand

345 – 354

10

Beta strand

362 – 368

7

Helix

373 – 375

3

Beta strand

377 – 382

6

Beta strand

384 – 389

6

Turn

390 – 392

3

Beta strand

393 – 396

4

Beta strand

403 – 405

3

Beta strand

408 – 412

5

Beta strand

417 – 424

8

Beta strand

427 – 429

3

Beta strand

433 – 436

4

Beta strand

460 – 462

3

Beta strand

466 – 473

8

Beta strand

476 – 480

5

Helix

482 – 484

3

Helix

488 – 491

4

Beta strand

496 – 504

9

Helix

506 – 510

5

Beta strand

516 – 519

4

Turn

520 – 522

3

Beta strand

523 – 527

5

Turn

529 – 531

3

Beta strand

534 – 536

3

Beta strand

538 – 544

7

Sequences

	Sequence		Length	Mass (Da)
	P00962-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E720164EF990F335	FASTA	554	63,478
	10 20 30 40 50 60 MSEAEARPTN FIRQIIDEDL ASGKHTTVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYKG 70 80 90 100 110 120 QCNLRFDDTN PVKEDIEYVE SIKNDVEWLG FHWSGNVRYS SDYFDQLHAY AIELINKGLA 130 140 150 160 170 180 YVDELTPEQI REYRGTLTQP GKNSPYRDRS VEENLALFEK MRAGGFEEGK ACLRAKIDMA 190 200 210 220 230 240 SPFIVMRDPV LYRIKFAEHH QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL 250 260 270 280 290 300 YDWVLDNITI PVHPRQYEFS RLNLEYTVMS KRKLNLLVTD KHVEGWDDPR MPTISGLRRR 310 320 330 340 350 360 GYTAASIREF CKRIGVTKQD NTIEMASLES CIREDLNENA PRAMAVIDPV KLVIENYQGE 370 380 390 400 410 420 GEMVTMPNHP NKPEMGSRQV PFSGEIWIDR ADFREEANKQ YKRLVLGKEV RLRNAYVIKA 430 440 450 460 470 480 ERVEKDAEGN ITTIFCTYDA DTLSKDPADG RKVKGVIHWV SAAHALPVEI RLYDRLFSVP 490 500 510 520 530 540 NPGAADDFLS VINPESLVIK QGFAEPSLKD AVAGKAFQFE REGYFCLDSR HSTAEKPVFN 550 RTVGLRDTWA KVGE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Escherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity." Uemura H., Conley J., Yamao F., Rogers J., Soell D.G. Protein Seq. Data Anal. 1:479-485(1988) [PubMed: 2464170] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene." Yamao F., Inokuchi H., Cheung A., Ozeki H., Soell D.G. J. Biol. Chem. 257:11639-11643(1982) [PubMed: 6288695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"Misaminoacylation by glutaminyl-tRNA synthetase: relaxed specificity in wild-type and mutant enzymes." Hoben P., Uemura H., Yamao F., Cheung A., Swanson R., Sumner-Smith M., Soell D. Fed. Proc. 43:2972-2976(1984) [PubMed: 6389180] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[8]	"Escherichia coli glutaminyl-tRNA synthetase. II. Characterization of the glnS gene product." Hoben P., Royal N., Cheung A., Yamao F., Biemann K., Soell D. J. Biol. Chem. 257:11644-11650(1982) [PubMed: 6749844] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-6, CHARACTERIZATION. Strain: K12.
[9]	"Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8-A resolution." Rould M.A., Perona J.J., Soell D., Steitz T.A. Science 246:1135-1142(1989) [PubMed: 2479982] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[10]	"Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase." Rould M.A., Perona J.J., Steitz T.A. Nature 352:213-218(1991) [PubMed: 1857417] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[11]	"How glutaminyl-tRNA synthetase selects glutamine." Rath V.L., Silvian L.F., Beijer B., Sproat B.S., Steitz T.A. Structure 6:439-449(1998) [PubMed: 9562563] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[12]	"Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases." Sherlin L.D., Bullock T.L., Newberry K.J., Lipman R.S., Hou Y.M., Beijer B., Sproat B.S., Perona J.J. J. Mol. Biol. 299:431-446(2000) [PubMed: 10860750] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

V01575 Genomic DNA. Translation: CAA24894.1.
U00096 Genomic DNA. Translation: AAC73774.1.
AP009048 Genomic DNA. Translation: BAA35328.1.
M16470, M16368 Genomic DNA. Translation: AAA69006.1.

PIR

SYECQT. G64802.
I41235.

RefSeq

AP_001318.1.
NP_415206.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EUQ	X-ray	3.10	A	1-548	[»]
1EUY	X-ray	2.60	A	1-548	[»]
1EXD	X-ray	2.70