Q2SX36 (SYE_BURTA) 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:	BTH_I1984

Organism

Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]

Taxonomic identifier

271848 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	469 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
Subunit structure	Monomer By similarity. HAMAP MF_00022_B
Subcellular location	Cytoplasm 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 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: 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 469	469	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000237349
Regions
	Motif	11 – 21	11	"HIGH" region HAMAP MF_00022_B
	Motif	243 – 247	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	246	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2SX36 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: EEE0D68248D730E0	FASTA	469	52,046
	10 20 30 40 50 60 MTRPVRTRFA PSPTGFIHLG NIRSALYPWA FARKMKGTFV LRIEDTDVER SSQEAVDAIL 70 80 90 100 110 120 EGMAWLGLDY DEGPYYQMQR MDRYREVLAQ MQEKGLVYPC YMSTEELDAL RERQRAAGEK 130 140 150 160 170 180 PRYDGTWRPE PGKVLPEPPA GVAPVLRFRN PLTGTVAWDD AVKGRVEISN EELDDLVVAR 190 200 210 220 230 240 PDGTPMYNFC VVVDDLDMGI THVIRGDDHV NNTPRQINIL RALGGEVPVY AHLPTVLNEQ 250 260 270 280 290 300 GEKMSKRHGA MSVMGYRDAG YLPEAVLNYL ARLGWSHGDA EIFTREQFVE WFDLEHLGKS 310 320 330 340 350 360 PAQYDHNKLN WLNNHYIKEA DDARLAGLAK PFFAALGIDA GAIEQGPDLV SVMGLMKDRA 370 380 390 400 410 420 STVKEIAENS AMFYRAPAPG ADALAQHVTD AVRPALVEFA AALKTVEWTK EAIAAALKAV 430 440 450 460 LGAHKLKMPQ LAMPVRLLVA GTTHTPSIDA VLLLFGRDVV VSRIEAALA

References

[1]

"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies." Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D. BMC Genomics 6:174-174(2005) [PubMed: 16336651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000086 Genomic DNA. Translation: ABC37833.1.
RefSeq	YP_442513.1. NC_007651.1.
3D structure databases
ProteinModelPortal	Q2SX36.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2SX36.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3850087.
GenomeReviews	Gene locus BTH_I1984 in contig CP000086_GR.
KEGG	bte:BTH_I1984.
PATRIC	19307002. VBIBurTha36512_4795.
TIGR	BTH_I1984.
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	ANFNDES.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	BTHA271848:BTH_I1984-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_BURTA

Accession

Primary (citable) accession number: Q2SX36

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	January 24, 2006
Last modified:	January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program