Q1IY50 (SYE_DEIGD) 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:	Dgeo_1539

Organism

Deinococcus geothermalis (strain DSM 11300) [Complete proteome] [HAMAP]

Taxonomic identifier

319795 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	480 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 – 480	480	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000330967
Regions
	Motif	9 – 19	11	"HIGH" region HAMAP MF_00022_B
	Motif	253 – 257	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	256	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1IY50 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: F7944E6653C2C491	FASTA	480	54,347
	10 20 30 40 50 60 MSVVTRIAPS PTGDPHVGTA YIGLFNHTLA QQARARGEEG KFILRIEDTD RNRYVPDSER 70 80 90 100 110 120 RIFQMMAWLG LTPDESPLQG GPNGPYRQSE RTAIYGEYAR KLVEAGHAYY AFETPEELAA 130 140 150 160 170 180 LREAAQQEGR VIAVPSRDLD PAEAQRRVDA GESAVIRLKV PREGETVVND ALRKPIAFQN 190 200 210 220 230 240 REIDDKVLLK ADGYPTYHLA NVVDDHLMGV THVIRAEEWI TSTPIHVLLY RAFGWAEPIF 250 260 270 280 290 300 AHMPLLRNAD KSKISKRKNP TSVEWYMAQG FLPEAMLNFL ATMGWTHPEG KEIFDLAEFQ 310 320 330 340 350 360 RVFRLEDVTL GGPVFSLDKL RWMNGKYLRE VLSEEEVAER LHAYLASQKH DLPDDDYFRA 370 380 390 400 410 420 VVRMMIPRMD VFSEFLEKTP YFWSEDYPVS EKAQHLIEEG RPFLPELAAR LKNLPSFDPA 430 440 450 460 470 480 TTEAALRAFA EERGLKPGKV MQPLRAAIAG TSESPGMFEL LEVLGQERVV ARVERAARGG

References

[1]

"Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P. Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 11300.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000359 Genomic DNA. Translation: ABF45834.1.
RefSeq	YP_605003.1. NC_008025.1.
3D structure databases
ProteinModelPortal	Q1IY50.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1IY50.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4057425.
GenomeReviews	Gene locus Dgeo_1539 in contig CP000359_GR.
KEGG	dge:Dgeo_1539.
NMPDR	fig|68909.1.peg.1677.
PATRIC	21625007. VBIDeiGeo41128_2133.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	ANFNDES.
PhylomeDB	Q1IY50.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	DGEO319795:DGEO_1539-MONOMER.
Family and domain databases
HAMAP	MF_00022_B. Glu_tRNA_synth_B. [Tree]
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR020752. aa-tRNA-synth_I_codon-bd_sub1. 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:1.10.8.70. aa-tRNA-synth_I_codon-bd_sub1. 1 hit. 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_DEIGD

Accession

Primary (citable) accession number: Q1IY50

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	June 13, 2006
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program