Q5ZU96 (SYE_LEGPH) 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:	lpg1911

Organism

Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) [Complete proteome] [HAMAP]

Taxonomic identifier

272624 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella › Legionella pneumophila › Legionella pneumophila subsp. pneumophila

Protein attributes

Sequence length	470 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
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.
Sequence caution	The sequence AAU27981.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
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 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 – 470	470	Glutamate--tRNA ligase HAMAP-Rule MF_00022		PRO_0000119587
Regions
	Motif	9 – 19	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	236 – 240	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	239	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5ZU96 [UniParc]. Last modified June 7, 2005. Version 2. Checksum: 37B2F48A462D198D	FASTA	470	53,574
	10 20 30 40 50 60 MTVRTRFAPS PTGFLHVGGV RTALFSWLYA KHHNGQFILR IEDTDRERST QESVQAILDG 70 80 90 100 110 120 MAWLGLNFDE GPYYQTERYA RYQQVAQQLL EEGKAYRCQC SKERLEALRE AQLAAKEKPR 130 140 150 160 170 180 YDGHCRNQSL PDSGIPYVIR FRNPDAGIVS FHDEVYGDIH VDNSELDDLI LVRSDGHPTY 190 200 210 220 230 240 NFAVVIDDWD MKITHVIRGD DHINNTPRQI NLFKALDAPV PVFAHLPMIL GEDGKRLSKR 250 260 270 280 290 300 HGAVSVLQFK ELGVLPHALL NYLVRLGWSH GDQEIFSVQE MITSFDLKNV SRGVSSFNYD 310 320 330 340 350 360 KLYWLNQHYQ KSDSPESVAN ALQWHFEQAG IDLNQGPDLK DLVAVQAERC KSLAEMCQIS 370 380 390 400 410 420 QYFYTDIIEY NEDAVKKHLR PVVLEPLMVL HERLKALDEW KNDKIQECIN DVSLQFDLNL 430 440 450 460 470 GKIAQPLRVA VTGSGTSPSI DMTLALLGKN KSIKRLEDAL EKIRARASVV

References

[1]

"The genomic sequence of the accidental pathogen Legionella pneumophila." Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S. , Georghiou A., Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A., Russo J.J. Science 305:1966-1968(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Philadelphia 1 / ATCC 33152 / DSM 7513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017354 Genomic DNA. Translation: AAU27981.1. Different initiation.
RefSeq	YP_095928.1. NC_002942.5.
3D structure databases
ProteinModelPortal	Q5ZU96.
ModBase	Search...
Protein-protein interaction databases
STRING	272624.lpg1911.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAU27981; AAU27981; lpg1911.
GeneID	3078160.
KEGG	lpn:lpg1911.
PATRIC	22330968. VBILegPne29832_1996.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252722.
KO	K01885.
OMA	WENVRVR.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	LPNE272624:GHDI-1934-MONOMER.
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_LEGPH

Accession

Primary (citable) accession number: Q5ZU96

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program