A8LCV4 (SYE_FRASN) 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:	Franean1_1684

Organism

Frankia sp. (strain EAN1pec) [Complete proteome] [HAMAP]

Taxonomic identifier

298653 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Frankineae › Frankiaceae › Frankia

Protein attributes

Sequence length	500 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
Cofactor	Binds 1 zinc ion per subunit By similarity. 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 Metal-binding Nucleotide-binding Zinc
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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 500	500	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000367675
Regions
	Motif	12 – 22	11	"HIGH" region HAMAP MF_00022_B
	Motif	235 – 239	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Metal binding	103	1	Zinc By similarity
	Metal binding	105	1	Zinc By similarity
	Metal binding	125	1	Zinc By similarity
	Metal binding	127	1	Zinc By similarity
	Binding site	238	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8LCV4 [UniParc]. Last modified December 4, 2007. Version 1. Checksum: F2A1947B86FCD570	FASTA	500	53,900
	10 20 30 40 50 60 MSTGRVRVRF APSPTGIFHV GGARSALFNW LVAKGAGGDF VLRVEDTDAS RNRPEWTEGI 70 80 90 100 110 120 ISALDWLGIS PGGYEGPVFQ SERAGRHAEA AAGLFAAGRA YYCGCTRDEL AARTGNAQHG 130 140 150 160 170 180 YDGFCRERGL GPGPGRALRF RTPDEGTTVV LDVIRGTPEF PNDTIEDFVI ARADGSAVFL 190 200 210 220 230 240 LANVVDDLDM GITHVVRGEE HLSNTPKQQL LWAALGTPPP VWAHVPVIVN EKRQKLSKRR 250 260 270 280 290 300 DKVALESYRA EGYLAAAMCN YLMLLGWAPP GDEEIVPFET IEASFRLEDV KPSPAFFDEK 310 320 330 340 350 360 KLRAFNGEYI RALSVDEFVA ACEPWLVPAA DVPAAVDAPA AAGTGDGAAG VTTAVPAPPW 370 380 390 400 410 420 SPERFSAEVF AAVAPLAQSR VAVLSEIVPM VDFLFLPEAP TDEAAWAKTM KGPALDLLTE 430 440 450 460 470 480 AAEAYEKVAW DHDVLRETLI EVGERHGLKL GKAQAPVRVA VTGRTVGLPL FESLEILGRE 490 500 ETLRRLRAAV ERLDTAANPA

References

[1]

"Genome characteristics of facultatively symbiotic Frankia sp. strains reflect host range and host plant biogeography." Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P., Goltsman E., Huang Y. , Kopp O.R., Labarre L., Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R. Genome Res. 17:7-15(2007) [PubMed: 17151343] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: EAN1pec.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000820 Genomic DNA. Translation: ABW11122.1.
RefSeq	YP_001506028.1. NC_009921.1.
3D structure databases
ProteinModelPortal	A8LCV4.
ModBase	Search...
Protein-protein interaction databases
STRING	A8LCV4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5670086.
GenomeReviews	Gene locus Franean1_1684 in contig CP000820_GR.
KEGG	fre:Franean1_1684.
PATRIC	21936234. VBIFraSp51419_1730.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG628189.
OMA	ANFNDES.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	FSP1855:FRANEAN1_1684-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_FRASN

Accession

Primary (citable) accession number: A8LCV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	December 4, 2007
Last modified:	January 25, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program