P43818 (SYE_HAEIN) 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:	HI_0274

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Taxonomic identifier

71421 [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 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 – 480	480	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000119572
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)
	P43818 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: ABE5A203F9CF700F	FASTA	480	54,875
	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 QGIDTSNGPA LTEIVTMLAE 370 380 390 400 410 420 RCKTLKEMAR SSRYFFEEFE TFDEAAAKKH FKGNAAEALA KVKEKLTALS SWDLHSIHEA 430 440 450 460 470 480 IEQTAAELEV GMGKVGMPLR VAVTGSGQSP SMDVTLVGIG RDRVLARIQR AIDFIHAQNA

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC21940.1.
PIR	B64059.
RefSeq	NP_438443.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P43818.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	949397.
GenomeReviews	Gene locus HI_0274 in contig L42023_GR.
KEGG	hin:HI0274.
NMPDR	fig|71421.1.peg.259.
PATRIC	20189077. VBIHaeInf48452_0289.
TIGR	HI_0274.
Phylogenomic databases
HOGENOM	HBG628189.
OMA	IEWFNLD.
PhylomeDB	P43818.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0274-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_HAEIN

Accession

Primary (citable) accession number: P43818

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program