B2G868 (SYE_LACRJ) 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:	LAR_1134

Organism

Lactobacillus reuteri (strain JCM 1112) [Complete proteome] [HAMAP]

Taxonomic identifier

557433 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	501 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 By similarity 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 – 501	501	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_1000090084
Regions
	Motif	11 – 21	11	"HIGH" region HAMAP MF_00022_B
	Motif	257 – 261	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	260	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	B2G868 [UniParc]. Last modified June 10, 2008. Version 1. Checksum: 299495BBD03FBE6A	FASTA	501	58,350
	10 20 30 40 50 60 MDQKVRVRYA PSPTGFLHIG NAQSALFNYL FARHFDGTMV LRIEDTDTKR NVEDGEASQR 70 80 90 100 110 120 ENLHWLGIDW DEGPNKPNPK YAPYRQSERN KEGIYHKYIQ ELLDKGIAYK DYSTEEELAE 130 140 150 160 170 180 MRERQKANNE PPHYDGRWYG KSEEEQKAAE AKGLKPTIRF HFPKDHDYEW DDIARGHVSF 190 200 210 220 230 240 NSDNLGGDFI IEKSDGMPTY NFAVVVDDHT MDITHVLRGA DHISNTPKQI AIYEALGWEH 250 260 270 280 290 300 PTFCHIPLIF NPKTRKKLSK RDKDTLQFIS EYKKHGYLHE AIFNFIAFLG WSPVGEREIY 310 320 330 340 350 360 SKEELIKVYD PKRMSKAPAY FDQKKLDWMN AQYIKSMSID ELTDRTMELI KEGETEEAKR 370 380 390 400 410 420 LQSIPEEQLT ELLKKTIKVH QRDVNKLLEV IQYAWSYYTV LDQSFNYDLL KDNEDFANED 430 440 450 460 470 480 VLAVLKGLKA KLENGDDDLD YSQAIKEVGK DTGIKGRGLY FPLNLAFTGS TSAPQIYEIM 490 500 DIYSRDTDIE LLDRMIKAFE N

References

[1]

"Comparative genome analysis of Lactobacillus reuteri and Lactobacillus fermentum reveal a genomic island for reuterin and cobalamin production." Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T., Hattori M. DNA Res. 15:151-161(2008) [PubMed: 18487258] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JCM 1112.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP007281 Genomic DNA. Translation: BAG25650.1.
RefSeq	YP_001842130.1. NC_010609.1.
3D structure databases
ProteinModelPortal	B2G868.
ModBase	Search...
Protein-protein interaction databases
STRING	B2G868.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6231269.
GenomeReviews	Gene locus LAR_1134 in contig AP007281_GR.
KEGG	lrf:LAR_1134.
PATRIC	22259788. VBILacReu111271_1250.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG628189.
OMA	VRFRMPD.
ProtClustDB	PRK01406.
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	K09698.
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_LACRJ

Accession

Primary (citable) accession number: B2G868

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	June 10, 2008
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program