Reviewed, UniProtKB/Swiss-Prot A8A2Q2 (SYE_ECOHS)

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:	EcHS_A2537

Organism

Escherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]

Taxonomic identifier

331112 [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	Inferred from homology.

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) By similarity.
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm. HAMAP MF_00022
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

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
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 zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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_1000057193
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 By similarity
	Metal binding	100	1	Zinc By similarity
	Metal binding	125	1	Zinc By similarity
	Metal binding	127	1	Zinc By similarity
	Binding site	240	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8A2Q2-1 [UniParc]. Last modified October 23, 2007. 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

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000802 Genomic DNA. Translation: ABV06806.1.
RefSeq	YP_001459189.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5594442.
GenomeReviews	Gene locus EcHS_A2537 in contig CP000802_GR.
KEGG	ecx:EcHS_A2537.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A8A2Q2. MAHIPLI.
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_ECOHS

Accession

Primary (citable) accession number: A8A2Q2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	June 16, 2009
This is version 12 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)