B1MDQ5 (SYE_MYCA9) 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:	MAB_3298c

Organism

Mycobacterium abscessus (strain ATCC 19977 / DSM 44196) [Complete proteome] [HAMAP]

Taxonomic identifier

561007 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium chelonae group › Mycobacterium abscessus subgroup › Mycobacterium abscessus

Protein attributes

Sequence length	496 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-Rule MF_00022
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
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: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP glutamate-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 496	496	Glutamate--tRNA ligase HAMAP-Rule MF_00022		PRO_1000090091
Regions
	Motif	12 – 22	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	256 – 260	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	259	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	B1MDQ5 [UniParc]. Last modified April 29, 2008. Version 1. Checksum: F09F0D61315C53DD	FASTA	496	54,711
	10 20 30 40 50 60 MSNTKIRVRF CPSPTGTPHV GLIRTALFNW AYARHCGGDF VFRIEDTDAG RDSEESYLAI 70 80 90 100 110 120 LDALRWLGLD WDEGPEVGGP YEPYRQSQRK ELHREVVRKL LEAGEAYEAF STAEEVEARH 130 140 150 160 170 180 LAAGRNPKLG YDNYDRDLTE EQRAAFRAEG RDPVVRLRMP DHDITWNDLV RGETTFAAGV 190 200 210 220 230 240 VPDFALTRGN GDPLYTLVNP VDDALMKITH VLRGEDLLPS TPRQIALYEA MIRIGVTDSI 250 260 270 280 290 300 PAFAHLPSVL GEGTKKLSKR DPQSNLFLHR DRGFIPEGLL NYLALLGWSI ADDHDIFSLA 310 320 330 340 350 360 EMVTAFDVTD VNSNPARFDQ KKADAINAEH IRLLAPEEFV TRLRTYFAAH GHELGLDESA 370 380 390 400 410 420 FAVAADLVQT RIVVLGDAWG LLKFLNDDAY AIDPGAARKE LGEASLPVLD AAIGALESLE 430 440 450 460 470 480 AWTTPAIEGA LKSALIEGLE LKPRKAFGPL RVAVTGATVS PPLFESMELL GSGRTLTRLR 490 NARSWENGVG DQTDSG

References

[1]

"Acquisition of foreign virulence genes by the cystic fibrosis pathogen Mycobacterium abscessus." Genoscope Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., Gaillard J.L. Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 19977 / DSM 44196.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU458896 Genomic DNA. Translation: CAM63374.1.
RefSeq	YP_001704028.1. NC_010397.1.
3D structure databases
ProteinModelPortal	B1MDQ5.
ModBase	Search...
Protein-protein interaction databases
STRING	561007.MAB_3298c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAM63374; CAM63374; MAB_3298c.
GeneID	5967485.
KEGG	mab:MAB_3298c.
PATRIC	17978370. VBIMycAbs55940_3356.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252720.
KO	K01885.
OMA	YESMELL.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	MABS561007:GJTG-3314-MONOMER.
Family and domain databases
Gene3D	1.10.10.350. 1 hit. 1.10.1160.10. 1 hit. 3.40.50.620. 2 hits.
HAMAP	MF_00022_B. Glu_tRNA_synth_B.
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. IPR004527. Glu-tRNA-ligase_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]
PANTHER	PTHR10119. PTHR10119. 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_MYCA9

Accession

Primary (citable) accession number: B1MDQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	April 29, 2008
Last modified:	May 1, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program