Q4QNR5 (SYE_HAEI8) 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:	NTHI0382

Organism

Haemophilus influenzae (strain 86-028NP) [Complete proteome] [HAMAP]

Taxonomic identifier

281310 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

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
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 – 480	480	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000119573
Regions
	Motif	21 – 31	11	"HIGH" region HAMAP MF_00022_B
	Motif	248 – 252	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Metal binding	110	1	Zinc By similarity
	Metal binding	112	1	Zinc By similarity
	Metal binding	137	1	Zinc By similarity
	Metal binding	139	1	Zinc By similarity
	Binding site	251	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4QNR5 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: DB8806EE7266AA3A	FASTA	480	54,835
	10 20 30 40 50 60 MKLDAPFNLD PNVKVRTRFA PSPTGYLHVG GARTALYSWL YAKHNNGEFV LRIEDTDLER 70 80 90 100 110 120 STPEATAAII EGMEWLNLPW EHGPYYQTKR FDRYNQVIDE MIEQGLAYRC YCTKEHLEEL 130 140 150 160 170 180 RHTQEQNKEK PRYDRHCLHD HNHSPDEPHV VRFKNPTEGS VVFDDAVRGR IEISNSELDD 190 200 210 220 230 240 LIIRRTDGSP TYNFCVVVDD WDMGITHVVR GEDHINNTPR QINILKAIGA PIPTYAHVSM 250 260 270 280 290 300 INGDDGQKLS KRHGAVSVMQ YRDDGYLPEA LINYLVRLGW GHGDQEIFSR EEMINYFELD 310 320 330 340 350 360 HVSKSASAFN TEKLQWLNQH YIRELPPEYV AKHLEWHYKD QSIDTSNGPA LTDIVSMLAE 370 380 390 400 410 420 RCKTLKEMAS SSRYFFEEFE TFDEAAAKKH FKGNAAEALA KVKEKLTALS SWNLHSIHEA 430 440 450 460 470 480 IEQTAAELEV GMGKVGMPLR VAVTGSGQSP SMDVTLVGIG RDRVLVRIQR AIDFIHAQNA

References

[1]

"Genomic sequence of an otitis media isolate of nontypeable Haemophilus influenzae: comparative study with H. influenzae serotype d, strain KW20." Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B., Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O., Munson R.S. Jr. J. Bacteriol. 187:4627-4636(2005) [PubMed: 15968074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 86-028NP.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000057 Genomic DNA. Translation: AAX87332.1.
RefSeq	YP_247992.1. NC_007146.2.
3D structure databases
ProteinModelPortal	Q4QNR5.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4QNR5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3429707.
GenomeReviews	Gene locus NTHI0382 in contig CP000057_GR.
KEGG	hit:NTHI0382.
PATRIC	20180933. VBIHaeInf100748_0348.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	IEWFNLD.
PhylomeDB	Q4QNR5.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	HINF281310:NTHI0382-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_HAEI8

Accession

Primary (citable) accession number: Q4QNR5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	July 19, 2005
Last modified:	January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program