Q1D8Y1 (SYE_MYXXD) 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:	MXAN_2675

Organism

Myxococcus xanthus (strain DK 1622) [Complete proteome] [HAMAP]

Taxonomic identifier

246197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Myxococcus

Protein attributes

Sequence length	479 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 – 479	479	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000330984
Regions
	Motif	11 – 21	11	"HIGH" region HAMAP MF_00022_B
	Motif	250 – 254	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Metal binding	108	1	Zinc By similarity
	Metal binding	110	1	Zinc By similarity
	Metal binding	135	1	Zinc By similarity
	Metal binding	137	1	Zinc By similarity
	Binding site	253	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1D8Y1 [UniParc]. Last modified July 11, 2006. Version 1. Checksum: A4EB8C0F73405E51	FASTA	479	53,209
	10 20 30 40 50 60 MPPALRVRFA PSPTGYLHIG GARTALMNFL QARRQGGTFV LRMEDTDQGR STPESVQAIL 70 80 90 100 110 120 DGLNWLGIDW DEGPGKEGPY APYFQMQRLD TYRKHADQLI AEGKAYRCYC TKEDLDAQRQ 130 140 150 160 170 180 VAEKAGGAFK YPGTCRERTE PPAGRNAADA VIRFKMPAGD GSVSFTDKAL GTITKTHSDL 190 200 210 220 230 240 DDWVMMRADG IPVYNFGCVI DDHLMDITLV ARGQEHVNST FPQLMLYQAL GWTPPDFAHL 250 260 270 280 290 300 PLILGPDREK LSKRKHPEAD VMVHKRNGVM PEALLNFVIR LGWSHGNDEV ISREQMLEWF 310 320 330 340 350 360 DFSDVGTTSG VWNPEKLLWL NQQWMKQLPV ETVVERLLPF LEAKGIQAKG DPRLETLVRT 370 380 390 400 410 420 LRERSNTLED IATTAANVYF RSGITLDEKA ATKHLSGESL NLLRKVRETL TALPEWSVEA 430 440 450 460 470 LDGVVKQVSE ASSVGMGKVA QPIRVALTGN TTSPGIGETL VLVGRDESLL RIDAALTRG

References

[1]

"Evolution of sensory complexity recorded in a myxobacterial genome." Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J., Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A. , Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B. Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006) [PubMed: 17015832] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DK 1622.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000113 Genomic DNA. Translation: ABF89409.1.
RefSeq	YP_630892.1. NC_008095.1.
3D structure databases
ProteinModelPortal	Q1D8Y1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1D8Y1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4103882.
GenomeReviews	Gene locus MXAN_2675 in contig CP000113_GR.
KEGG	mxa:MXAN_2675.
PATRIC	22647885. VBIMyxXan43560_2627.
TIGR	MXAN_2675.
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	NATIIEM.
PhylomeDB	Q1D8Y1.
Enzyme and pathway databases
BioCyc	MXAN246197:MXAN_2675-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_MYXXD

Accession

Primary (citable) accession number: Q1D8Y1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	July 11, 2006
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program