B6JH82 (SYE_OLICO) 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:	OCAR_5972, OCA5_c20520

Organism

Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5) [Complete proteome] [HAMAP]

Taxonomic identifier

504832 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Oligotropha › Oligotropha carboxidovorans

Protein attributes

Sequence length	473 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. HAMAP-Rule MF_00022
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00022.
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: UniProtKB-HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-HAMAP glutamate-tRNA ligase activity Inferred from electronic annotation. Source: UniProtKB-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 – 473	473	Glutamate--tRNA ligase HAMAP-Rule MF_00022		PRO_1000090094
Regions
	Motif	11 – 21	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	240 – 244	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	243	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	B6JH82 [UniParc]. Last modified December 16, 2008. Version 1. Checksum: 0641DCF01364B4C4	FASTA	473	52,213
	10 20 30 40 50 60 MTEPVVTRFA PSPTGFLHIG GARTALFNWL YARKQGGKML LRIEDTDRER STDAAIKAIL 70 80 90 100 110 120 DGLNWLGIEW DGEVIYQFSR AARHREVAEQ LLAEGKAYRC YATPEELTKM REAARAEGRA 130 140 150 160 170 180 VRYDGRWRDR DPSEAPADVK PVIRLKAPQT GETVIEDQVQ GRVVWQNENL DDLVLLRSDG 190 200 210 220 230 240 TPTYMLAVVV DDHDMGVTHV IRGDDHLINA ARQKHIYDAL GWTVPTMAHI PLIHGPDGSK 250 260 270 280 290 300 LSKRHGALGV EAYRTMGYLP AALRNYLVRL GWSHGDQEIF STSEMIEAFE LSGIGRSAAR 310 320 330 340 350 360 FDFAKLENLN GHYMRASGDA ELVKAFEDIL QFLPQGPALQ AKLNDTTRAQ LLQAMPGLKE 370 380 390 400 410 420 RAKTLLELID SAAYIFADRP LALDAKASAV LTPQVRALLG ELRSSLANVT DWNAANTEAA 430 440 450 460 470 MRAYAEKNNL KLGAVAQPLR AALTGRTTSP GIFDVLAVLG RDDALARLQD QAA

References

[1]	"Genome sequence of the chemolithoautotrophic bacterium Oligotropha carboxidovorans OM5T." Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L. J. Bacteriol. 190:5531-5532(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49405 / DSM 1227 / OM5.
[2]	"Complete genome sequences of the chemolithoautotrophic Oligotropha carboxidovorans strains OM4 and OM5." Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., Meyer O. J. Bacteriol. 193:5043-5043(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49405 / DSM 1227 / OM5.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001196 Genomic DNA. Translation: ACI93092.1. CP002826 Genomic DNA. Translation: AEI06759.1.
RefSeq	YP_002288957.1. NC_011386.1. YP_004633000.1. NC_015684.1.
3D structure databases
ProteinModelPortal	B6JH82.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
STRING	504832.OCAR_5972.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACI93092; ACI93092; OCAR_5972. AEI06759; AEI06759; OCA5_c20520.
GeneID	10847184. 6992110.
KEGG	oca:OCAR_5972. ocg:OCA5_c20520.
PATRIC	22805825. VBIOliCar134280_1870.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252722.
KO	K01885.
OMA	AFRCFCT.
OrthoDB	EOG6DRPF7.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	OCAR504832:GJPZ-2052-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_bac/mito. IPR000924. Glu/Gln-tRNA-synth. 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.
Pfam	PF00749. tRNA-synt_1c. 1 hit. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
SUPFAM	SSF48163. SSF48163. 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_OLICO

Accession

Primary (citable) accession number: B6JH82
Secondary accession number(s): F8BW48

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	December 16, 2008
Last modified:	February 19, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program