B1X9R9 (SYE_ECODH) 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:	ECDH10B_2564

Organism

Escherichia coli (strain K12 / DH10B) [Complete proteome] [HAMAP]

Taxonomic identifier

316385 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
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. HAMAP MF_00022_B
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00022_B
Subunit structure	Monomer By similarity. HAMAP MF_00022_B
Subcellular location	Cytoplasm By similarity HAMAP MF_00022_B.
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: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate-tRNA ligase activity Inferred from electronic annotation. Source: EC metal 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	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_1000090073
Regions
	Motif	9 – 19	11	"HIGH" region HAMAP MF_00022_B
	Motif	237 – 241	5	"KMSKS" region HAMAP MF_00022_B
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)
	B1X9R9 [UniParc]. Last modified May 20, 2008. 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 complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse." Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R. J. Bacteriol. 190:2597-2606(2008) [PubMed: 18245285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / DH10B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000948 Genomic DNA. Translation: ACB03554.1.
RefSeq	YP_001731332.1. NC_010473.1.
3D structure databases
ProteinModelPortal	B1X9R9.
SMR	B1X9R9. Positions 2-469.
ModBase	Search...
Protein-protein interaction databases
STRING	B1X9R9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000011356; EBESCP00000010884; EBESCG00000010418.
GeneID	6059993.
GenomeReviews	Gene locus ECDH10B_2564 in contig CP000948_GR.
KEGG	ecd:ECDH10B_2564.
PATRIC	18465005. VBIEscCol59506_2586.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009048.
HOGENOM	HBG628189.
OMA	MAHIPLI.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	ECOL316385:ECDH10B_2564-MONOMER.
Family and domain databases
HAMAP	MF_00022_B. Glu_tRNA_synth_B. [Tree]
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-synth_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]
Gene3D	G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits. G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KO	K01885.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 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...

Entry information

Entry name

SYE_ECODH

Accession

Primary (citable) accession number: B1X9R9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	May 20, 2008
Last modified:	January 25, 2012
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program