Q1AS60 (SYE2_RUBXD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase 2
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2

Gene names

Name:	gltX2
Ordered Locus Names:	Rxyl_2856

Organism

Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129) [Complete proteome] [HAMAP]

Taxonomic identifier

266117 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Rubrobacteridae › Rubrobacterales › Rubrobacterineae › Rubrobacteraceae › Rubrobacter

Protein attributes

Sequence length	496 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 – 496	496	Glutamate--tRNA ligase 2 HAMAP MF_00022_B		PRO_0000367768
Regions
	Motif	13 – 23	11	"HIGH" region HAMAP MF_00022_B
	Motif	255 – 259	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	258	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1AS60 [UniParc]. Last modified July 11, 2006. Version 1. Checksum: C10F241670F45A88	FASTA	496	56,617
	10 20 30 40 50 60 MEASRQVRVR YAPSPTGRLH VGGVRTALFN WLFARKHGGV FILRIEDTDL ERSTEESVEQ 70 80 90 100 110 120 LKRSLRWIGL DWDEGPDVGG PHAPYRQTER LELYRRAARR LLESGAAYYD FATPEELTRF 130 140 150 160 170 180 RQRARAEGRP PIYTGGPYRE MDPEEALRRV RMGEPHTVRF KTPREGRTVF EDIIRGPVGF 190 200 210 220 230 240 ENATIEDFVL LKSTGTPTYN FAAAVDDAEM QITHVIRGDD HISNTPRQIM IHRALGHELP 250 260 270 280 290 300 AFAHVPQVLG PDRKKLSKRH GAASVEDFAE QGILPEALFN YLALLGAGYA ADEEIFAPEE 310 320 330 340 350 360 LAERFRLEKV SGNPAIFDEQ KLLAINAVYI RRKSPEELAM LAAPMLSERG VADAGELERD 370 380 390 400 410 420 MPRLVRIMEL LRERLQRTTD IPEAAGYFYG ERLDYDREQF EKQFGKEFVR ENLPELYRRL 430 440 450 460 470 480 KALPEWTADA IESCVRGLAA EKEKGARHLI HPLRFATTGR TVSAGLFETM ELIGRERCLL 490 RIADVLERLQ SPERSL

References

[1]

"Complete sequence of Rubrobacter xylanophilus DSM 9941." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S., Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P. Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 9941 / NBRC 16129.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000386 Genomic DNA. Translation: ABG05768.1.
RefSeq	YP_645580.1. NC_008148.1.
3D structure databases
ProteinModelPortal	Q1AS60.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1AS60.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4115833.
GenomeReviews	Gene locus Rxyl_2856 in contig CP000386_GR.
KEGG	rxy:Rxyl_2856.
NMPDR	fig|266117.6.peg.2496.
PATRIC	23372512. VBIRubXyl52678_2828.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	FENATIE.
PhylomeDB	Q1AS60.
Enzyme and pathway databases
BioCyc	RXYL266117:RXYL_2856-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

SYE2_RUBXD

Accession

Primary (citable) accession number: Q1AS60

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	July 11, 2006
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program