Q72M46 (SYE_LEPIC) 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:	LIC_13345

Organism

Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) [Complete proteome] [HAMAP]

Taxonomic identifier

267671 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length	521 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 – 521	521	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000119590
Regions
	Motif	13 – 23	11	"HIGH" region HAMAP MF_00022_B
	Motif	253 – 257	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	256	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q72M46 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 995625A4A3D4F98A	FASTA	521	58,809
	10 20 30 40 50 60 MNQSKEVRTR FAPSPSGFLH VGGARTALFN YLYAKSQGGK FILRIEDTDQ NRSTEDSFKI 70 80 90 100 110 120 ILESLKWLGV NWDEGPEVGG EYGPYIQSQR LNIYKEYTEK LLKEKKAYRC FCTQEELEAK 130 140 150 160 170 180 KKQSEAMGVP YVYDGLHANM SDEEVQEKLK QGIPYSVRFK TPSKTLIIND IIQGKVKFET 190 200 210 220 230 240 KLIGDFIIVK SDGFPSYNYA VVVDDALMKI THVIRGVGHL SNTPRQILLY EALGYNIPEF 250 260 270 280 290 300 AHASEIVGMD GKKLSKRAGA TSILAFRDLG YLPETFRNYM ALLGWTSTDG REFLPGDELE 310 320 330 340 350 360 KIFDVHRCSK SPSTFDVFKK PKGSDEEVVT NFSDLTQIAE AMNPKSKLNW LSNRTIRDLN 370 380 390 400 410 420 ISKVLENLLP FLMDRKDIPA EVKNVNNPIL TSIVESVRVY LDNLTQAPDY VAEFFVTDLK 430 440 450 460 470 480 IQSEETIGFL KDGEGPKVVN EFYEILKNSD PKTDEDYKNL MSKVGEVTGQ KGKTLYMPIR 490 500 510 520 AATTGKSAGL ELPILFPLLG KEKLLQRIEK TSKETGISLS N

References

[1]

"Comparative genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis." Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S. , Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A. J. Bacteriol. 186:2164-2172(2004) [PubMed: 15028702] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Fiocruz L1-130.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016823 Genomic DNA. Translation: AAS71887.1.
RefSeq	YP_003250.1. NC_005823.1.
3D structure databases
ProteinModelPortal	Q72M46.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2771897.
GenomeReviews	Gene locus LIC_13345 in contig AE016823_GR.
KEGG	lic:LIC13345.
PATRIC	22379805. VBILepInt6257_4050.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG628189.
OMA	ANFNDES.
PhylomeDB	Q72M46.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	LINT267671:LIC_13345-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_LEPIC

Accession

Primary (citable) accession number: Q72M46

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 21, 2004
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program