Glutamine--tRNA ligase - glnS - Escherichia coli (strain K12)

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P00962 (SYQ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glutamine--tRNA ligase
EC=6.1.1.18

Alternative name(s):
Glutaminyl-tRNA synthetase
Short name=GlnRS

Gene names

Name:	glnS
Ordered Locus Names:	b0680, JW0666

Organism

Escherichia coli (strain K12) [Reference 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). HAMAP-Rule MF_00126
Subunit structure	Monomer.
Subcellular location	Cytoplasm HAMAP-Rule MF_00126.
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 Reference proteome
Gene Ontology (GO)
Biological_process	glutaminyl-tRNA aminoacylation Inferred from direct assay PubMed 16734422. Source: EcoCyc glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: UniProtKB-HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-HAMAP glutamine-tRNA ligase activity Inferred from direct assay PubMed 7506418. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.7 Ref.8

Chain

2 – 554

553

Glutamine--tRNA ligase HAMAP-Rule MF_00126

PRO_0000195833

Regions

Motif

34 – 44

"HIGH" region HAMAP-Rule MF_00126

Motif

268 – 272

"KMSKS" region HAMAP-Rule MF_00126

Sites

Binding site

271

ATP By similarity

Experimental info

Sequence conflict

549 – 554

WAKVGE → GRK Ref.2

Secondary structure

554

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00962 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E720164EF990F335
Show »

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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [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 277:1453-1462(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-6, CHARACTERIZATION. Strain: K12.
[9]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[10]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[11]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[12]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[13]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

NP_415206.1. NC_000913.3.
YP_488960.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj

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	A	1-548	[»]
1GSG	X-ray	2.80	P	2-554	[»]
1GTR	X-ray	2.50	A	2-554	[»]
1GTS	X-ray	2.80	A	2-554	[»]
1NYL	X-ray	2.60	A	9-547	[»]
1O0B	X-ray	2.70	A	2-554	[»]
1O0C	X-ray	2.70	A	2-554	[»]
1QRS	X-ray	2.60	A	2-554	[»]
1QRT	X-ray	2.70	A	2-554	[»]
1QRU	X-ray	3.00	A	2-554	[»]
1QTQ	X-ray	2.25	A	2-554	[»]
1ZJW	X-ray	2.50	A	2-554	[»]
2RD2	X-ray	2.60	A	1-548	[»]
2RE8	X-ray	2.60	A	1-548	[»]
4JXX	X-ray	2.30	A	2-554	[»]
4JXZ	X-ray	2.40	A	2-554	[»]
4JYZ	X-ray	2.50	A	2-554	[»]

ProteinModelPortal

P00962.

SMR

P00962. Positions 8-549.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

DIP

DIP-9787N.

IntAct

P00962. 5 interactions.

MINT

MINT-1227909.

STRING

511145.b0680.

Chemistry

BindingDB

P00962.

2D gel databases

SWISS-2DPAGE

P00962.

Proteomic databases

PaxDb

P00962.

PRIDE

P00962.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73774; AAC73774; b0680.
BAA35328; BAA35328; BAA35328.

GeneID

12932213.
945310.

KEGG

ecj:Y75_p0659.
eco:b0680.

PATRIC

32116549. VBIEscCol129921_0707.

Organism-specific databases

EchoBASE

EB0385.

EcoGene

EG10390. glnS.

Phylogenomic databases

eggNOG

COG0008.

HOGENOM

HOG000259232.

K01886.

OMA

SREIYID.

OrthoDB

EOG6DRPF7.

PhylomeDB

P00962.

Enzyme and pathway databases

BioCyc

EcoCyc:GLNS-MONOMER.
ECOL316407:JW0666-MONOMER.
MetaCyc:GLNS-MONOMER.

BRENDA

6.1.1.18. 2026.

SABIO-RK

P00962.

Gene expression databases

Genevestigator

P00962.

Family and domain databases

Gene3D

1.10.1160.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.

HAMAP

MF_00126. Gln_tRNA_synth.

InterPro

IPR001412. aa-tRNA-synth_I_CS.
IPR004514. Gln-tRNA-synth.
IPR022861. Gln_tRNA_ligase_bac.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

PANTHER

PTHR10119. PTHR10119. 1 hit.

Pfam

PF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]

PRINTS

PR00987. TRNASYNTHGLU.

SUPFAM

SSF50715. SSF50715. 1 hit.

TIGRFAMs

TIGR00440. glnS. 1 hit.

PROSITE

PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00962.

PRO

P00962.

Entry information

Entry name

SYQ_ECOLI

Accession

Primary (citable) accession number: P00962
Secondary accession number(s): Q59403

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	July 9, 2014
This is version 158 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents