Q668N0 (SYE_YERPS) 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:	YPTB2707

Organism

Yersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP]

Taxonomic identifier

273123 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia › Yersinia pseudotuberculosis

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-Rule MF_00022
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW tRNA binding Inferred from electronic annotation. Source: InterPro
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-Rule MF_00022		PRO_0000119709
Regions
	Motif	9 – 19	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	237 – 241	5	"KMSKS" region HAMAP-Rule 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)
	Q668N0 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 92591583BDB9582C	FASTA	471	53,182
	10 20 30 40 50 60 MKIKTRFAPS PTGYLHVGGA RTALYSWLFS RHLGGEFVLR IEDTDLERST QEAIDAIMDG 70 80 90 100 110 120 MNWLNLDWDE GPYFQTKRFD RYNAVIDQML DAGTAYRCYC SKERLEALRE AQMANGEKPR 130 140 150 160 170 180 YDGHCRDSQC THGADEPSVV RFRNPQEGSV IFDDKIRGPI EFSNQELDDL IIRRTDGSPT 190 200 210 220 230 240 YNFCVVIDDW DMEITHVIRG EDHINNTPRQ INILKALGAP VPEYAHVSMI LGDDGKKLSK 250 260 270 280 290 300 RHGAVGVMQY RDDGYLPEAL LNYLVRLGWS HGDQEIFSIE EMTQLFTLDA VSKSASAFNT 310 320 330 340 350 360 EKLQWLNHHY INSLPPEQVA VHLSWHVEQL GIDTRNGPEL VEIVKLLGER CKTLKEMAES 370 380 390 400 410 420 CRYFYEEFDA FDVDAAKKHL RPIARQPLEA VKVKLAAITE WTTENVHNAI QGTADELGVG 430 440 450 460 470 MGKVGMPLRV AVTGVGQSPG MDVTVHAIGQ ARTLARIDKA LAFISEREAQ Q

References

[1]

"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis." Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E. Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IP32953.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX936398 Genomic DNA. Translation: CAH21945.1.
RefSeq	YP_071217.1. NC_006155.1.
3D structure databases
ProteinModelPortal	Q668N0.
ModBase	Search...
Protein-protein interaction databases
STRING	273123.YPTB2707.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAH21945; CAH21945; YPTB2707.
GeneID	2955725.
KEGG	yps:YPTB2707.
PATRIC	18644495. VBIYerPse22266_3300.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252722.
KO	K01885.
OMA	RYRDFKG.
ProtClustDB	PRK01406.
Family and domain databases
Gene3D	1.10.10.350. 1 hit. 1.10.1160.10. 1 hit. 3.40.50.620. 2 hits.
HAMAP	MF_00022_B. Glu_tRNA_synth_B.
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-ligase_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]
PANTHER	PTHR10119. PTHR10119. 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_YERPS

Accession

Primary (citable) accession number: Q668N0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program