Q5NHY6 (SYE_FRATT) 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:	FTT_0307

Organism

Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)

Taxonomic identifier

177416 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Francisellaceae › Francisella

Protein attributes

Sequence length	468 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 Reference 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 – 468	468	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000119564
Regions
	Motif	8 – 18	11	"HIGH" region HAMAP MF_00022_B
	Motif	236 – 240	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Metal binding	97	1	Zinc By similarity
	Metal binding	99	1	Zinc By similarity
	Metal binding	124	1	Zinc By similarity
	Metal binding	126	1	Zinc By similarity
	Binding site	239	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5NHY6 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: B5D3AC570C11C4A2	FASTA	468	52,953
	10 20 30 40 50 60 MITTRFAPSP TGFLHVGGVR TALFSWLYAK NNNGKFILRI EDTDLERSTQ EAVDAILDGM 70 80 90 100 110 120 SWLGLKNDGE IYYQTKRFDR YKEVIQELIA DGKAYYCSCS KERLEELREY QQANNLKTGY 130 140 150 160 170 180 DGKCRDANYI PQQGESYVVR FKNPQDGVVS WDDAVKGRIS ISNHELDDMI IQRADGSPTY 190 200 210 220 230 240 NFCVVVDDID MAITHIIRGD DHVNNTPKQI NIYKALNANV PIFAHVPMIL GPDGAKLSKR 250 260 270 280 290 300 HGAVNVMQYR EDGYLPQAIL NYLVRLGWSH GDQEIFSIEE MIKAFNLEHI NASPSRFDFE 310 320 330 340 350 360 KLKWLNKHYI KESKFDDIQT EVEYHFAKTG LDISNGPDLK ELVAVMAEKV DTLVELAEKS 370 380 390 400 410 420 SYFYSDDISY DENAVKKHIK ASTGEIFVKL LENFEALDAQ QWQDPDVLHN IVSTTAEQCQ 430 440 450 460 VGMGKVGMPL RVAITGSGQS PDIGITLKLL GKNKVVARLT KALEELCK

References

[1]

"The complete genome sequence of Francisella tularensis, the causative agent of tularemia." Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H., Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D., Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S., Sjoestedt A. , Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W., Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W. Nat. Genet. 37:153-159(2005) [PubMed: 15640799] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SCHU S4 / Schu 4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ749949 Genomic DNA. Translation: CAG44940.1.
RefSeq	YP_169356.1. NC_006570.2.
3D structure databases
ProteinModelPortal	Q5NHY6.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q5NHY6. 10 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3191767.
GenomeReviews	Gene locus FTT_0307 in contig AJ749949_GR.
KEGG	ftu:FTT_0307.
Phylogenomic databases
HOGENOM	HBG628189.
OMA	ANFNDES.
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	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_FRATT

Accession

Primary (citable) accession number: Q5NHY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	February 1, 2005
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program