O33120 (SYE_MYCLE) 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
Synonyms:	gltS
Ordered Locus Names:	ML1688
ORF Names:	MLCB637.29

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	502 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 – 502	502	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000119603
Regions
	Motif	21 – 31	11	"HIGH" region HAMAP MF_00022_B
	Motif	265 – 269	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	268	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	O33120 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: F618C748C9F24A60	FASTA	502	55,305
	10 20 30 40 50 60 MTAVTSDGTP QAAKVRVRFC PSPTGVPHVG MVRTALFNWA YARHTGGTFV LRIEDTDADR 70 80 90 100 110 120 DSEESYLALL DALRWLGLNW DEGPEVGGPY GPYRQSQRTD IYREVVAKLL ATGEAYYAFS 130 140 150 160 170 180 TPEEVENRHL AAGRNPKLGY DNFDRDLTDA QFSAYLAEGR KPVVRLRMPD EDISWDDLVR 190 200 210 220 230 240 GTTTFAVGTV PDYVLTRASG DPLYTLVNPC DDALMKITHV LRGEDLLSST PRQVALYQAL 250 260 270 280 290 300 IRIGMAERIP EFGHFPSVLG EGTKKLSKRE PQSNLFAHRD RGFIPEGLLN YLALLGWAIA 310 320 330 340 350 360 DDHDLFSLDE MVAAFDVVDV NSNPARFDQK KADAVNAEHI RMLDSEDFAG RLRDYFTTHG 370 380 390 400 410 420 YHIALDPANY EAGFVAAAQL VQTRIVVLGD AWDLLKFLND DEYSIDSKAA AKELDADAGP 430 440 450 460 470 480 VLDVACAVLD SLVDWTTASI EDVLKVALIE GLGLKPRKVF GPIRVAATGA LVSPPLFESL 490 500 ELLGRARSLQ RLSAARARVT SA

References

[1]

"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G. Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z99263 Genomic DNA. Translation: CAB16444.1. AL583923 Genomic DNA. Translation: CAC30641.1.
PIR	T45422.
RefSeq	NP_302160.1. NC_002677.1.
3D structure databases
ProteinModelPortal	O33120.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000028561; EBMYCP00000028167; EBMYCG00000028556.
GeneID	910058.
GenomeReviews	Gene locus ML1688 in contig AL450380_GR.
KEGG	mle:ML1688.
NMPDR	fig|272631.1.peg.1032.
PATRIC	18056506. VBIMycLep78757_3182.
Organism-specific databases
Leproma	ML1688.
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000016746.
HOGENOM	HBG628189.
OMA	MAHIPLI.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	MLEP272631:ML1688-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_MYCLE

Accession

Primary (citable) accession number: O33120

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program