Q0RF57 (SYE_FRAAA) 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:	FRAAL5260

Organism

Frankia alni (strain ACN14a) [Complete proteome] [HAMAP]

Taxonomic identifier

326424 [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_1000001899
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)
	Q0RF57 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: A3B2118E7A675150	FASTA	470	51,235
	10 20 30 40 50 60 MGSGRVRVRF APSPTGIFHV GGARSALFNW LVALRAGGDF VLRVEDTDAS RNRPEWTDGI 70 80 90 100 110 120 ISALDWLGIS PGRYEGPVLQ SSRADRHRAA AVRLREAGLA YFCDCTREAL AERTGNAQHG 130 140 150 160 170 180 YDGFCRDRGL EPGPGRALRF RTPDDGVTTV HDLIRGTPEF PNDTIEDFVI ARADGSAVFL 190 200 210 220 230 240 LANVVDDLEM GITHVIRGEE HLSNTPKQQL LWAALGAAEP PVWAHVPVIV NEKRQKLSKR 250 260 270 280 290 300 RDKVALESYR DEGYLPGAMK NYLMLLGWAP SGDDEIVPWE TIESTFDLAD VKPSPAFFDE 310 320 330 340 350 360 KKLRAFNGEY IRALSVEEFI AAVEPWLAPP AAPWAADAFD AGTFAAVAGL AQSRVSVLAE 370 380 390 400 410 420 IVPMVDFLFL PAAPVDDAAW AKAMKGPAAQ LLADVHDVFG KIEWDAETLK ATLAELGERH 430 440 450 460 470 GLKLAKAQAP VRVAVTGRTV GLPLFESLEV FGREATRRRI AAARDRLAAG

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: ACN14a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CT573213 Genomic DNA. Translation: CAJ63893.1.
RefSeq	YP_715425.1. NC_008278.1.
3D structure databases
ProteinModelPortal	Q0RF57.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0RF57.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4233601.
GenomeReviews	Gene locus FRAAL5260 in contig CT573213_GR.
KEGG	fal:FRAAL5260.
PATRIC	21919740. VBIFraAln347_4821.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	TEYIRAY.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	FALN326424:FRAAL5260-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_FRAAA

Accession

Primary (citable) accession number: Q0RF57

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program