Reviewed, UniProtKB/Swiss-Prot P04805 (SYE_ECOLI)

Names and origin

Protein names

Recommended name:
    Glutamyl-tRNA synthetase
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase
      Short name=GluRS

Gene names

Name:	gltX
Ordered Locus Names:	b2400, JW2395

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.7 Ref.8
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). Ref.6
Cofactor	Binds 1 zinc ion per subunit. Ref.6 Ref.9
Enzyme regulation	Inhibited by 1,10-phenanthroline. Ref.6
Subunit structure	Monomer. Ref.1
Subcellular location	Cytoplasm. HAMAP MF_00022
Miscellaneous	This is the smallest aminoacyl-tRNA synthetase of E.coli; it does not bind glutamate in the absence of cognate tRNA, which is therefore required for activation of the amino acid substrate. HAMAP MF_00022
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.
biophysicochemical properties	Kinetic parameters: KM=0.32 µM for tRNA(Glu) HAMAP MF_00022 KM=0.105 mM for Glu

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	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: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP glutamate-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ydfR	P76160	1	EBI-549949,EBI-544071

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 471	471	Glutamyl-tRNA synthetase HAMAP MF_00022		PRO_0000119555
Regions
	Motif	9 – 19	11	"HIGH" region HAMAP MF_00022
	Motif	237 – 241	5	"KMSKS" region HAMAP MF_00022
Sites
	Metal binding	98	1	Zinc HAMAP MF_00022
	Metal binding	100	1	Zinc HAMAP MF_00022
	Metal binding	125	1	Zinc HAMAP MF_00022
	Metal binding	127	1	Zinc HAMAP MF_00022
	Binding site	240	1	ATP By similarity
Experimental info
	Mutagenesis	98	1	C → S: 10-fold decrease in activity. Strong decrease in zinc content. Ref.9
	Mutagenesis	100	1	C → S: Loss of activity. Strong decrease in zinc content. Ref.9 Ref.10
	Mutagenesis	100	1	C → Y: Does not prevent zinc binding. Reduces only 2-fold the binding affinity for tRNA(Glu), but reduces more than 10-fold the affinity for glutamate in the presence of tRNA(Glu). Ref.9 Ref.10
	Mutagenesis	125	1	C → S: Loss of activity. Strong decrease in zinc content. Ref.9
	Mutagenesis	127	1	H → Q: 10-fold decrease in activity. Strong decrease in zinc content. Ref.9
	Mutagenesis	129	1	H → Q: No change in activity and in zinc content. Ref.9
	Mutagenesis	131	1	H → Q: No change in activity and in zinc content. Ref.9
	Mutagenesis	132	1	H → Q: No change in activity and in zinc content. Ref.9
	Mutagenesis	138	1	C → S: No change in activity and in zinc content. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P04805-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 8264A799E5383398	FASTA	471	53,816
	10 20 30 40 50 60 MKIKTRFAPS PTGYLHVGGA RTALYSWLFA RNHGGEFVLR IEDTDLERST PEAIEAIMDG 70 80 90 100 110 120 MNWLSLEWDE GPYYQTKRFD RYNAVIDQML EEGTAYKCYC SKERLEALRE EQMAKGEKPR 130 140 150 160 170 180 YDGRCRHSHE HHADDEPCVV RFANPQEGSV VFDDQIRGPI EFSNQELDDL IIRRTDGSPT 190 200 210 220 230 240 YNFCVVVDDW DMEITHVIRG EDHINNTPRQ INILKALKAP VPVYAHVSMI NGDDGKKLSK 250 260 270 280 290 300 RHGAVSVMQY RDDGYLPEAL LNYLVRLGWS HGDQEIFTRE EMIKYFTLNA VSKSASAFNT 310 320 330 340 350 360 DKLLWLNHHY INALPPEYVA THLQWHIEQE NIDTRNGPQL ADLVKLLGER CKTLKEMAQS 370 380 390 400 410 420 CRYFYEDFAE FDADAAKKHL RPVARQPLEV VRDKLAAITD WTAENVHHAI QATADELEVG 430 440 450 460 470 MGKVGMPLRV AVTGAGQSPA LDVTVHAIGK TRSIERINKA LDFIAERENQ Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Glutamyl-tRNA synthetase of Escherichia coli. Isolation and primary structure of the gltX gene and homology with other aminoacyl-tRNA synthetases." Breton R., Sanfacon H., Papayannopoulos I., Biemann K., Lapointe J. J. Biol. Chem. 261:10610-10617(1986) [PubMed: 3015933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT.
[2]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"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.
[4]	"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.
[5]	"Closely spaced and divergent promoters for an aminoacyl-tRNA synthetase gene and a tRNA operon in Escherichia coli. Transcriptional and post-transcriptional regulation of gltX, valU and alaW." Brun V., Sanfacon H., Breton R., Lapointe J. J. Mol. Biol. 214:845-864(1990) [PubMed: 2201777] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
[6]	"The glutamyl-tRNA synthetase of Escherichia coli contains one atom of zinc essential for its native conformation and its catalytic activity." Liu J., Lin S.-X., Blochet J.-E., Pezolet M., Lapointe J. Biochemistry 32:11390-11396(1993) [PubMed: 8218204] [Abstract] Cited for: PROTEIN SEQUENCE OF 112-116, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION.
[7]	"The catalytic mechanism of glutamyl-tRNA synthetase of Escherichia coli. Evidence for a two-step aminoacylation pathway, and study of the reactivity of the intermediate complex." Kern D., Lapointe J. Eur. J. Biochem. 106:137-150(1980) [PubMed: 6280993] [Abstract] Cited for: FUNCTION.
[8]	"The catalytic mechanism of the glutamyl-tRNA synthetase from Escherichia coli. Detection of an intermediate complex in which glutamate is activated." Kern D., Lapointe J. J. Biol. Chem. 255:1956-1961(1980) [PubMed: 6986385] [Abstract] Cited for: FUNCTION.
[9]	"The zinc-binding site of Escherichia coli glutamyl-tRNA synthetase is located in the acceptor-binding domain. Studies by extended x-ray absorption fine structure, molecular modeling, and site-directed mutagenesis." Liu J., Gagnon Y., Gauthier J., Furenlid L., L'Heureux P.-J., Auger M., Nureki O., Yokoyama S., Lapointe J. J. Biol. Chem. 270:15162-15169(1995) [PubMed: 7797500] [Abstract] Cited for: COFACTOR, ZINC-BINDING SITES, MUTAGENESIS OF CYS-98; CYS-100; CYS-125; HIS-127; HIS-129; HIS-131; HIS-132 AND CYS-138.
[10]	"The zinc-binding site of a class I aminoacyl-tRNA synthetase is a SWIM domain that modulates amino acid binding via the tRNA acceptor arm." Banerjee R., Dubois D.Y., Gauthier J., Lin S.-X., Roy S., Lapointe J. Eur. J. Biochem. 271:724-733(2004) [PubMed: 14764088] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-100.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X63976 Genomic DNA. Translation: CAA45391.1. M13687 Genomic DNA. Translation: AAA65715.1. U00096 Genomic DNA. Translation: AAC75457.1. AP009048 Genomic DNA. Translation: BAA16272.1. X55737 Genomic DNA. Translation: CAA39269.1.
PIR	SYECET. A25956.
RefSeq	AP_002997.1. NP_416899.1.
3D structure databases
HSSP	HSSP built from PDB template 1J09 based on UniProtKB P27000.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:9810N.
IntAct	P04805. 16 interactions.
2-D gel databases
ECO2DBASE	F047.8. 6TH EDITION.
Genome annotation databases
GeneID	946906.
GenomeReviews	Gene locus JW2395 in contig AP009048_GR. Gene locus b2400 in contig U00096_GR.
KEGG	ecj:JW2395. eco:b2400.
Organism-specific databases
EchoBASE	EB0402.
EcoGene	EG10407. gltX.
CMR	Search...
Phylogenomic databases
HOGENOM	P04805.
OMA	P04805. MAHIPLI.
Enzyme and pathway databases
BioCyc	EcoCyc:GLURS-MON. MetaCyc:GLURS-MON.
Family and domain databases
HAMAP	MF_00022. [Tree]
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR001412. aa-tRNA-synth_I_CS. IPR004527. Glu-tRNA-synth_Ic_bac/mito. IPR000924. Glu/Gln-tRNA-synth_Ic. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 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_ECOLI

Accession

Primary (citable) accession number: P04805

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	June 16, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)