P0C6Q1 (SYE_VIBCH) 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:	VC_2214

Organism

Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]

Taxonomic identifier

243277 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › Vibrio cholerae › Vibrio cholerae O1 › Vibrio cholerae O1 biovar El Tor

Protein attributes

Sequence length	474 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 AAF95358.1 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 – 474	474	Glutamate--tRNA ligase HAMAP-Rule MF_00022		PRO_0000119691
Regions
	Motif	9 – 19	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	240 – 244	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	243	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0C6Q1 [UniParc]. Last modified March 18, 2008. Version 1. Checksum: D7F6FC1B9CDF5146	FASTA	474	53,379
	10 20 30 40 50 60 MTVKTRFAPS PTGYLHVGGA RTALYSWLYA KSQGGEFVLR IEDTDLERST QAAVDAIIEG 70 80 90 100 110 120 MTWLGLEWDE GPYYQTKRFD RYNQVIDQLL AEGKAYKCYA PKELLDEIRA EQEANKEMPR 130 140 150 160 170 180 YDANHPKIKA VNDAAKEGEP CCIRFRNPKE GSVVFDDQIR GRIEIRNDQL DDLIIRRTDG 190 200 210 220 230 240 TPTYNFCVVV DDVDMGISHV IRGEDHINNT PRQINIYKAM GATIPTFAHC AMILGDDGAK 250 260 270 280 290 300 LSKRHGAVSV MQYRDDGYLP EALLNYLVRL GWGHGDQEIF SRDEMINLFS LNAISKSASA 310 320 330 340 350 360 FNTDKLLWLN NHYIKTSEPE YVAKHLEWHF ENQGINKATG PALAEVVKLV GERCNTLVEL 370 380 390 400 410 420 AQQSRYFYED FAEFDADAAK KHLRGVAKEP LMLALSKIEA LTEWNTEALH HVIAQVCEEL 430 440 450 460 470 EIGMGKIGMP LRVAVTGGGQ SPSVDAVMNL IGQERVIARI KMALEYIETR EANA

References

[1]

"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M. Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE003852 Genomic DNA. Translation: AAF95358.1. Different initiation.
PIR	G82104.
RefSeq	NP_231845.1. NC_002505.1.
3D structure databases
ProteinModelPortal	P0C6Q1.
ModBase	Search...
Protein-protein interaction databases
STRING	243277.VC2214.
Proteomic databases
PRIDE	P0C6Q1.
Protocols and materials databases
DNASU	2613253.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF95358; AAF95358; VC_2214.
GeneID	2613253.
KEGG	vch:VC2214.
PATRIC	20083473. VBIVibCho83274_2112.
Phylogenomic databases
eggNOG	COG0008.
KO	K01885.
OMA	RYRDFKG.
ProtClustDB	PRK01406.
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. IPR001412. aa-tRNA-synth_I_CS. 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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYE_VIBCH

Accession

Primary (citable) accession number: P0C6Q1
Secondary accession number(s): O31153, Q9KPZ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 18, 2008
Last modified:	May 1, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program