A0QUY7 (SYE_MYCS2) 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:	MSMEG_2383

Organism

Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)

Taxonomic identifier

246196 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 486	486	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000330980
Regions
	Motif	12 – 22	11	"HIGH" region HAMAP MF_00022_B
	Motif	256 – 260	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	259	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0QUY7 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: 4A7B779612605BBC	FASTA	486	54,019
	10 20 30 40 50 60 MTTKKVRVRF CPSPTGTPHV GLVRTALFNW AYARHTGGDF VFRIEDTDAA RDSDESYAAI 70 80 90 100 110 120 LDALRWLGMD WDEGPEVGGP YEPYRQSQRR EIYRDVVARL LEAGEVYEAY STPEEVEARH 130 140 150 160 170 180 LAAGRNPKLG YDNYDRDLTD AQRKAFADEG RRPVLRLRMP DEDLSWNDLV RGPTTFAAGS 190 200 210 220 230 240 VPDFAITRSN GDPLYTLVNP VDDALMKITH VLRGEDILPS TPRQIALYRA LMRIGVAEFV 250 260 270 280 290 300 PEFAHLPSVL GEGNKKLSKR DPQSNLFLHR DRGFIPEGLL NYLALLGWGI ADDHDVFSLD 310 320 330 340 350 360 EMVAAFDVAD VNSNPARFDQ KKADAINAEH IRMLAPEDFT ARLREYFVTH GYDTTLDDAA 370 380 390 400 410 420 FAEAAALVQT RVVVLGDAWG LLKFFNDDAY EIDEKSAAKE LKPESAAVLD AALSALEAVG 430 440 450 460 470 480 DWTTPAIEAA LKTALLEGLE LKPRKAFGPI RVAVTGAAVS PPLFESMELL GRDRSLARLR AARDRV

References

[1]	Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155.
[2]	"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol." Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O. Genome Res. 19:128-135(2009) [PubMed: 18955433] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000480 Genomic DNA. Translation: ABK74186.1.
RefSeq	YP_886725.1. NC_008596.1.
3D structure databases
ProteinModelPortal	A0QUY7.
ModBase	Search...
Protein-protein interaction databases
STRING	A0QUY7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000043516; EBMYCP00000041853; EBMYCG00000043511.
GeneID	4533604.
GenomeReviews	Gene locus MSMEG_2383 in contig CP000480_GR.
KEGG	msm:MSMEG_2383.
NMPDR	fig|246196.1.peg.2382.
PATRIC	18077190. VBIMycSme59918_2349.
TIGR	MSMEG_2383.
Phylogenomic databases
eggNOG	COG0008.
GeneTree	EBGT00050000016746.
HOGENOM	HBG628189.
OMA	ESIIQFV.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	MSME246196:MSMEG_2383-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. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYE_MYCS2

Accession

Primary (citable) accession number: A0QUY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	January 9, 2007
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