Q6MKR6 (SYE_BDEBA) 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:	Bd2319

Organism

Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) [Complete proteome] [HAMAP]

Taxonomic identifier

264462 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Bdellovibrionales › Bdellovibrionaceae › Bdellovibrio › Bdellovibrio bacteriovorus

Protein attributes

Sequence length	490 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.

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 – 490	490	Glutamate--tRNA ligase HAMAP-Rule MF_00022		PRO_0000119514
Regions
	Motif	15 – 25	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	259 – 263	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	262	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6MKR6 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 93CFE5194BA53A1E	FASTA	490	55,717
	10 20 30 40 50 60 MSSKISPHVR VRFAPSPTGY LHVGGARTAL YNYLFAKKNG GEFILRIEDT DEARSTQESL 70 80 90 100 110 120 RGVVDDLVWL GLKWDEGVDP VTLKDVGPNG PYRQSERLHI YKEIADQLLK EGKAYYCFMT 130 140 150 160 170 180 EEDIEKQKAA AGSFAHLVSP YQDWTLDQAL ERLKTGDKAV VRFKTKNLVK DYIFTDLVRG 190 200 210 220 230 240 EVKFPSDMVG DFVLLRSDGM PVYNFCCVVD DHLMKMTHVF RAEEHLPNTL RQLMIYEAMN 250 260 270 280 290 300 WPTPEFGHMA LILDEDRQKL SKRKGAVACG QLKDEGYLAS AVLNFIALLG WSDPQGREIL 310 320 330 340 350 360 SVKDMLEVFD ISRLNPSGAI FDRVKFKWMN AQHLRALPNA ELWQAVAPFL ARENMDLPTD 370 380 390 400 410 420 PAWQSKSLDL FKPYMEILAD AIELYRPLND KSYVILPEAD ETLKWESTKA VLTSWKNLLQ 430 440 450 460 470 480 AHPSDYMTEE EFLKMQDEVK NQTGSKGKHL FMPIRVAVIG KPHGAELKTL VPLMKKSSLV 490 ARAEQALAKV

References

[1]

"A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective." Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C. Science 303:689-692(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15356 / DSM 50701 / NCIB 9529 / HD100.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842652 Genomic DNA. Translation: CAE80141.1.
RefSeq	NP_969148.1. NC_005363.1.
3D structure databases
ProteinModelPortal	Q6MKR6.
ModBase	Search...
Protein-protein interaction databases
STRING	264462.Bd2319.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAE80141; CAE80141; Bd2319.
GeneID	2735761.
KEGG	bba:Bd2319.
PATRIC	21079114. VBIBdeBac73187_2120.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252720.
KO	K01885.
OMA	ESIIQFV.
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_BDEBA

Accession

Primary (citable) accession number: Q6MKR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program