A5VKT4 (SYE_LACRD) 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:	Lreu_1201

Organism

Lactobacillus reuteri (strain DSM 20016) [Complete proteome] [HAMAP]

Taxonomic identifier

557436 [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 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_1000057196
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)
	A5VKT4 [UniParc]. Last modified July 10, 2007. 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]

"The evolution of host specialization in the vertebrate gut symbiont Lactobacillus reuteri." Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M., Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M., Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L. , Ivanova N., Kyrpides N.C., Walter J. PLoS Genet. 7:E1001314-E1001314(2011) [PubMed: 21379339] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 20016.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000705 Genomic DNA. Translation: ABQ83458.1.
RefSeq	YP_001271795.1. NC_009513.1.
3D structure databases
ProteinModelPortal	A5VKT4.
ModBase	Search...
Protein-protein interaction databases
STRING	A5VKT4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5189240.
GenomeReviews	Gene locus Lreu_1201 in contig CP000705_GR.
KEGG	lre:Lreu_1201.
PATRIC	22255604. VBILacReu87937_1214.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG628189.
OMA	VRFRMPD.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	LREU557436:LREU_1201-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	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_LACRD

Accession

Primary (citable) accession number: A5VKT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	July 10, 2007
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program