Q03U68 (SYE1_LACBA) 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
Ordered Locus Names:	LVIS_0080

Organism

Lactobacillus brevis (strain ATCC 367 / JCM 1170) [Complete proteome] [HAMAP]

Taxonomic identifier

387344 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	503 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 By similarity 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 – 503	503	Glutamate--tRNA ligase 1 HAMAP MF_00022_B		PRO_0000367695
Regions
	Motif	17 – 27	11	"HIGH" region HAMAP MF_00022_B
	Motif	261 – 265	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	264	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q03U68 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: F4FED28A21F61247	FASTA	503	57,736
	10 20 30 40 50 60 MSENSTVKKN VRVRYAPSPT GFLHIGNAQS ALFNYLFARH YHGTMVLRIE DTDVKRNVPH 70 80 90 100 110 120 GEDSQIDNLH WLGIDWDEGP DKPNPKYAPY HQTERQDLYH RYITQLLDQG LAYKDYATED 130 140 150 160 170 180 ELTTMRDQQR AAGEAPHYDG RWYGRSVADQ QAAEARGLKP SIRLHLPANH EYAWDDIIKG 190 200 210 220 230 240 HVAFNSDNMG GDFIIEKSNG MPTYNFAVVI DDYLMDITDV LRGDDHIANT PKQIAVYEAL 250 260 270 280 290 300 GLKHPNFGHI TLIYNPKTRK KLSKRDKETL QFISQYKNQG YLSEAIFNFI AFLGWSPEGE 310 320 330 340 350 360 DELFSREELI ERYDPARMSK SPAYFDQSKL DWINAAYIKR LDLDDMTDRV LELVDEGQTD 370 380 390 400 410 420 VARQVKALQL PDLRTLTSQV CKIYQTEIHQ LSEIMDKVLF YVTILQEPLD YDQLRQFDRT 430 440 450 460 470 480 ATLAVLTAFR KHVQALPVDV ATPDFKKMIQ TVSQETGVTG RNLYFPLNVA FTGDHSAPQI 490 500 DEVLRLFANS TIIELLTKAI AHV

References

[1]

"Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed: 17030793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 367 / JCM 1170.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000416 Genomic DNA. Translation: ABJ63254.1.
RefSeq	YP_794285.1. NC_008497.1.
3D structure databases
ProteinModelPortal	Q03U68.
ModBase	Search...
Protein-protein interaction databases
STRING	Q03U68.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4412658.
GenomeReviews	Gene locus LVIS_0080 in contig CP000416_GR.
KEGG	lbr:LVIS_0080.
NMPDR	fig|387344.8.peg.77.
PATRIC	22199128. VBILacBre134470_0079.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	EGPNEGG.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	LBRE387344:LVIS_0080-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	K09698.
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_LACBA

Accession

Primary (citable) accession number: Q03U68

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program