Q47SA6 (SYE_THEFY) 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:	Tfu_0623

Organism

Thermobifida fusca (strain YX) [Complete proteome] [HAMAP]

Taxonomic identifier

269800 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptosporangineae › Nocardiopsaceae › Thermobifida

Protein attributes

Sequence length	477 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
Cofactor	Binds 1 zinc ion per subunit By similarity. 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 Metal-binding Nucleotide-binding Zinc
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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 477	477	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000237415
Regions
	Motif	12 – 22	11	"HIGH" region HAMAP MF_00022_B
	Motif	238 – 242	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Metal binding	106	1	Zinc By similarity
	Metal binding	108	1	Zinc By similarity
	Metal binding	128	1	Zinc By similarity
	Metal binding	130	1	Zinc By similarity
	Binding site	241	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q47SA6 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: 82327E88C794893F	FASTA	477	53,668
	10 20 30 40 50 60 MTDKAIRTRF APSPTGMFHV GGARSALFNW ALALQQPEGK FVLRIEDTDA ARNRPEWTEG 70 80 90 100 110 120 ILRALSALGI DERDPHFEGP YFQSAYADKH REVAEELYRK GRAYYCDCTR EQIQERRGNP 130 140 150 160 170 180 HLGYDGYCRD RGLEPGPGRA LRFRVPEGGP TVVDDKIRGR VEFDHSAIED FVIARSDGSP 190 200 210 220 230 240 LFVLANVVDD VEMAITHVVR GEEHLSNTPK QQLLWEALGQ TPPVWAHLPV IVNEKRQKLS 250 260 270 280 290 300 KRRDKVALED YLAEGYLPEA MVNYLMLLGW GPGDDREIMP FSEMVPLFRL EDVNSSSAFF 310 320 330 340 350 360 DEKKLRAFNG EYIRALDTTE FVERCAPWLG SEKAPWPAEN FDAQVFEAVA PLAQTRISVL 370 380 390 400 410 420 SEIVSYVDFL FLDRPVEDEK SWAKAMKPGV GEEMLTAALE RFSDPNLEWR AEPLKAALEE 430 440 450 460 470 VAAAQGLKLG KAQAPVRVAV TGRTVGLPLF ESLELLGRSR VQERLRAALE KLKAAGE

References

[1]

"Genome sequence and analysis of the soil cellulolytic actinomycete Thermobifida fusca YX." Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B., Kyrpides N. J. Bacteriol. 189:2477-2486(2007) [PubMed: 17209016] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: YX.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000088 Genomic DNA. Translation: AAZ54661.1.
RefSeq	YP_288684.1. NC_007333.1.
3D structure databases
ProteinModelPortal	Q47SA6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q47SA6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3580652.
GenomeReviews	Gene locus Tfu_0623 in contig CP000088_GR.
KEGG	tfu:Tfu_0623.
NMPDR	fig|269800.4.peg.619.
PATRIC	23901684. VBITheFus33945_0647.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	ANFNDES.
PhylomeDB	Q47SA6.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	TFUS269800:TFU_0623-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	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_THEFY

Accession

Primary (citable) accession number: Q47SA6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	September 13, 2005
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program