Q8NQX9 (SYE_CORGL) 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
Synonyms:	gltS
Ordered Locus Names:	Cgl1293, cg1463

Organism

Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]

Taxonomic identifier

196627 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › Corynebacterium glutamicum

Protein attributes

Sequence length	493 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-Rule MF_00022
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.
Sequence caution	The sequence CAF19995.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP glutamate-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 493	493	Glutamate--tRNA ligase HAMAP-Rule MF_00022		PRO_0000119549
Regions
	Motif	10 – 20	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	254 – 258	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	257	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8NQX9 [UniParc]. Last modified April 30, 2003. Version 2. Checksum: 38EB2B2CE1BC5A14	FASTA	493	55,391
	10 20 30 40 50 60 MTDVRVRFCP SPTGTPHVGL VRTALFNWAY ARHTGGKLVF RIEDTDAARD SEESYSAIID 70 80 90 100 110 120 SLRWLGMDWD EGVEKGGPHE PYRQSQRKDI YQDVLKQLID AGEVYPAYST AEEVEERHKA 130 140 150 160 170 180 AGRDPKLGYD NFDRDLTEEQ VAAFEAEGRK PVWRLRMPEQ DWKWTDLVRG EVEFKSFTQP 190 200 210 220 230 240 DFVVARSNGE PLYTLVNPVD DALMEVTHVL RGEDLLPSTP RQLALYEALK RIGVAKATPA 250 260 270 280 290 300 FGHLPFVMGE GNKKLSKRDP QSSLFNHRDN GIIPEGMLNY LALLGWSLSA DQDIFGVDEL 310 320 330 340 350 360 IANFDVADVL GNPARFDQKK LEAINADHIR LLEPKDFEAR LRAYMTEYTE FPADYPAEKF 370 380 390 400 410 420 AIAAELVQTR IKVLSEAWDL LKFLVTADED LVFNEKAAKK NLKETAVEPL NAGIAALEAV 430 440 450 460 470 480 EEWTTPNIEA ALNKALIEDL GLKPRVAFGA LRIGISGEAV SPPLFESMEL LGKESTLVRL 490 KVTREQTPFV VAE

References

[1]

"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes." Ikeda M., Nakagawa S. Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

[2]

"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000036 Genomic DNA. Translation: BAB98686.1. BX927151 Genomic DNA. Translation: CAF19995.1. Different initiation.
RefSeq	NP_600515.1. NC_003450.3. YP_225581.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q8NQX9.
ModBase	Search...
Protein-protein interaction databases
STRING	196627.cg1463.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB98686; BAB98686; BAB98686. CAF19995; CAF19995; cg1463.
GeneID	1019274. 3344640.
KEGG	cgb:cg1463. cgl:NCgl1244.
PATRIC	21494628. VBICorGlu203724_1270.
Phylogenomic databases
eggNOG	COG0008.
KO	K01885.
OMA	YESMELL.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	CGLU196627:GJDM-1277-MONOMER.
Family and domain databases
Gene3D	1.10.10.350. 1 hit. 1.10.1160.10. 1 hit. 3.40.50.620. 2 hits.
HAMAP	MF_00022_B. Glu_tRNA_synth_B.
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. IPR004527. Glu-tRNA-ligase_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]
PANTHER	PTHR10119. PTHR10119. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYE_CORGL

Accession

Primary (citable) accession number: Q8NQX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	April 30, 2003
Last modified:	May 1, 2013
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program