Q8G0S1 (SYE1_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase 1
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1

Gene names

Name:	gltX1
Synonyms:	gltX2
Ordered Locus Names:	BR1016, BS1330_I1012

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	457 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 – 457	457	Glutamate--tRNA ligase 1 HAMAP MF_00022_B		PRO_0000119525
Regions
	Motif	9 – 19	11	"HIGH" region HAMAP MF_00022_B
	Motif	250 – 254	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	253	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8G0S1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 4C98329D7800A0C1	FASTA	457	50,772
	10 20 30 40 50 60 MTVTVRFAPS PTGYIHIGNT RTALSNWLYA SKNNGKFILR YDDTDVERSK DEYAQAIAVD 70 80 90 100 110 120 LDWLGVRPDR VEYQSKRFDI YAKAVEKLKT AGLLYACYET ADELERRRKL RLARRLPPVY 130 140 150 160 170 180 GREALKLTDA EKAALEAEGR KPHWRFLLPN FESDPFATQR TEVHWDDLVR GPQTVDLASM 190 200 210 220 230 240 SDPILVREDG TYLYTLPSVV DDIDMGVTHI IRGDDHVTNT GVQISIFKAL GATPPVFGHH 250 260 270 280 290 300 NLLTTISGEG LSKRTGALSV GSLREAGYEP MAVASLAILI GTSESVTAAP DMAALAEHFD 310 320 330 340 350 360 LASISKSSAK FDPSELDALN RSLLHEMPFE KAKPRLEALG ICGAKAESFW LAVRGNLDRF 370 380 390 400 410 420 SDVSDWWQVV SGDLPEAPDL SGEDRDFVRH AFDLLPPEPW NGQTWKSWTE AVKSATGRKG 430 440 450 KNLFMPLRLA LTGQAHGPEL ADLLVLVGLE RTKSRRP

References

[1]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014291 Genomic DNA. Translation: AAN29938.1. CP002997 Genomic DNA. Translation: AEM18356.1.
RefSeq	NP_698023.1. NC_004310.3.
3D structure databases
ProteinModelPortal	Q8G0S1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1166689.
GenomeReviews	Gene locus BR1016 in contig AE014291_GR.
KEGG	bms:BR1016.
NMPDR	fig|204722.1.peg.980.
PATRIC	17790342. VBIBruSui107850_1027.
TIGR	BR1016.
Phylogenomic databases
HOGENOM	HBG628189.
OMA	DQERIEW.
ProtClustDB	PRK12558.
Enzyme and pathway databases
BioCyc	BSUI204722:BR_1016-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

SYE1_BRUSU

Accession

Primary (citable) accession number: Q8G0S1
Secondary accession number(s): G0K9U0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program