Q9XCL6 (SYE_PSEAE) 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:	PA3134

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]

Taxonomic identifier

208964 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas aeruginosa group › Pseudomonas aeruginosa

Protein attributes

Sequence length	494 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 Reference 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 – 494	494	Glutamate--tRNA ligase HAMAP-Rule MF_00022		PRO_0000119627
Regions
	Motif	10 – 20	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	251 – 255	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Metal binding	107	1	Zinc By similarity
	Metal binding	109	1	Zinc By similarity
	Metal binding	134	1	Zinc By similarity
	Metal binding	136	1	Zinc By similarity
	Binding site	254	1	ATP By similarity
Experimental info
	Sequence conflict	93	1	K → R in AAD33773. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9XCL6 [UniParc]. Last modified December 8, 2000. Version 2. Checksum: EC3EFD97BA5AFD72	FASTA	494	56,749
	10 20 30 40 50 60 MTTVRTRIAP SPTGDPHVGT AYIALFNLCF ARQHGGQFIL RIEDTDQLRS TRESEQQIYD 70 80 90 100 110 120 ALRWLGIEWD EGPDVGGPHG PYRQSERGHI YKKYSDELVE KGHAFTCFCT PERLDAVRAE 130 140 150 160 170 180 QMARKETPRY DGHCMHLPKD EVQRRLAAGE SHVTRMKVPT EGVCVVPDML RGDVEIPWDR 190 200 210 220 230 240 MDMQVLMKAD GLPTYFLANV VDDHLMGITH VLRGEEWLPS APKLIKLYEY FGWEQPQLCY 250 260 270 280 290 300 MPLLRNPDKS KLSKRKNPTS ITFYERMGYL PQALLNYLGR MGWSMPDERE KFTLAEMIEH 310 320 330 340 350 360 FDLSRVSLGG PIFDLEKLSW LNGQWIREQS VEEFAREVQK WALNPEYLMK IAPHVQGRVE 370 380 390 400 410 420 NFSQIAPLAG FFFSGGVPLD ASLFEHKKLD PTQVRQVLQL VLWKLESLRQ WEKERITGCI 430 440 450 460 470 480 QAVAEHLQLK LRDVMPLMFP AITGHASSVS VLDAMEILGA DLSRYRLRQA LELLGGASKK 490 ETKEWEKIRD AIPG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the glutamyl-tRNA synthetase (gltX) gene from Pseudomonas aeruginosa." Franklund C.V., Goldberg J.B. J. Bacteriol. 181:3582-3586(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PAK.
[2]	"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V. Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF139107 Genomic DNA. Translation: AAD33773.1. AE004091 Genomic DNA. Translation: AAG06522.1.
PIR	E83254.
RefSeq	NP_251824.1. NC_002516.2.
3D structure databases
ProteinModelPortal	Q9XCL6.
SMR	Q9XCL6. Positions 4-471.
ModBase	Search...
Protein-protein interaction databases
STRING	208964.PA3134.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	882647.
KEGG	pae:PA3134.
PATRIC	19840849. VBIPseAer58763_3286.
Organism-specific databases
PseudoCAP	PA3134.
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252720.
KO	K01885.
OMA	ESIIQFV.
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_PSEAE

Accession

Primary (citable) accession number: Q9XCL6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	December 8, 2000
Last modified:	May 1, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program