O86528 (SYE_STRCO) 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:	SCO5547
ORF Names:	SC1C2.28

Organism

Streptomyces coelicolor

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	494 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 Reference 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 – 494	494	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000119663
Regions
	Motif	15 – 25	11	"HIGH" region HAMAP MF_00022_B
	Motif	260 – 264	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Metal binding	112	1	Zinc By similarity
	Metal binding	114	1	Zinc By similarity
	Metal binding	139	1	Zinc By similarity
	Metal binding	141	1	Zinc By similarity
	Binding site	263	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	O86528 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: AC3F4EF4D58D0FAB	FASTA	494	54,917
	10 20 30 40 50 60 MASASGSPVR VRFCPSPTGN PHVGLVRTAL FNWAFARHHQ GTLVFRIEDT DAARDSEESY 70 80 90 100 110 120 DQLLDSMRWL GFDWDEGPEV GGPHAPYRQS QRMDIYQDVA QKLLDAGHAY RCYCSQEELD 130 140 150 160 170 180 TRREAARAAG KPSGYDGHCR ELTDAQVEEY TSQGREPIVR FRMPDEAITF TDLVRGEITY 190 200 210 220 230 240 LPENVPDYGI VRANGAPLYT LVNPVDDALM EITHVLRGED LLSSTPRQIA LYKALIELGV 250 260 270 280 290 300 AKEIPAFGHL PYVMGEGNKK LSKRDPQSSL NLYRERGFLP EGLLNYLSLL GWSLSADQDI 310 320 330 340 350 360 FTIEEMVAAF DVSDVQPNPA RFDLKKCEAI NGDHIRLLEV KDFTERCRPW LKAPVAPWAP 370 380 390 400 410 420 EDFDEAKWQA IAPHAQTRLK VLSEITDNVD FLFLPEPVFD EASWTKAMKE GSDALLTTAR 430 440 450 460 470 480 EKLDAADWTS PEALKEAVLA AGEAHGLKLG KAQAPVRVAV TGRTVGLPLF ESLEVLGKEK 490 ALARIDAALA RLAA

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL939124 Genomic DNA. Translation: CAA19995.1.
PIR	T29077.
RefSeq	NP_629681.1. NC_003888.3.
3D structure databases
ProteinModelPortal	O86528.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1100987.
GenomeReviews	Gene locus SCO5547 in contig AL645882_GR.
KEGG	sco:SCO5547.
NMPDR	fig|100226.1.peg.5499.
PATRIC	23740958. VBIStrCoe124346_5635.
Phylogenomic databases
HOGENOM	HBG628189.
OMA	VRFRMPD.
PhylomeDB	O86528.
ProtClustDB	PRK01406.
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. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYE_STRCO

Accession

Primary (citable) accession number: O86528

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1998
Last modified:	January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program