Q2J816 (SYE_FRASC) 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:	Francci3_3219

Organism

Frankia sp. (strain CcI3) [Complete proteome] [HAMAP]

Taxonomic identifier

106370 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	470 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 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 – 470	470	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000237364
Regions
	Motif	12 – 22	11	"HIGH" region HAMAP MF_00022_B
	Motif	236 – 240	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	239	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2J816 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: F6BB857433665B83	FASTA	470	51,540
	10 20 30 40 50 60 MGSGRVRVRF APSPTGIFHV GGARSALFNW LVARRAGGDF VLRVEDTDAS RNRPEWTDGI 70 80 90 100 110 120 ISALDWLGIS PGGYEGPVLQ SSRADRHRAA AERLHAEGLA YYCDCTREAL AERTGNAQRG 130 140 150 160 170 180 YDGFCRDRGL APGPGRALRF RTPDDGVTIV EDLIRGTPEF PNETIEDFVV ARADGSAVFL 190 200 210 220 230 240 LANVVDDLEM GITHVIRGEE HLSNTPKQQL LWAALGADAP PVWAHVPVIV NEKRQKLSKR 250 260 270 280 290 300 RDKVALESYR DEGYLPAAMK NYLMLLGWAP PGEDEIVPWE TIESTFDLAD VKPSPAFFDE 310 320 330 340 350 360 KKLKAFNGEY IRRLSVAEFI EAVRPWLSAP AAPWEPAAFD ADAFAALAPL AQSRVSVLSE 370 380 390 400 410 420 IVPMVDFLFL PEAPIDDAAW AKAMKGPAAE LLADVHDLYD KIEWEAETLK AGLTEVGERH 430 440 450 460 470 GLKLGKAQAP VRVAVTGRSV GLPLFESLEA LGRETTLRRL AEARERLTGG

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: CcI3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000249 Genomic DNA. Translation: ABD12576.1.
RefSeq	YP_482305.1. NC_007777.1.
3D structure databases
ProteinModelPortal	Q2J816.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2J816.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3906185.
GenomeReviews	Gene locus Francci3_3219 in contig CP000249_GR.
KEGG	fra:Francci3_3219.
PATRIC	21929760. VBIFraSp10456_3492.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	SVKWLLN.
PhylomeDB	Q2J816.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	FSP106370:FRANCCI3_3219-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_FRASC

Accession

Primary (citable) accession number: Q2J816

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	March 7, 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