Q6A6M1 (SYE_PROAC) 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:	PPA1869

Organism

Propionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP]

Taxonomic identifier

267747 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Propionibacteriaceae › Propionibacterium › Propionibacterium acnes

Protein attributes

Sequence length	497 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.

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: 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 – 497	497	Glutamate--tRNA ligase HAMAP-Rule MF_00022		PRO_0000119623
Regions
	Motif	13 – 23	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	253 – 257	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	256	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6A6M1 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: 9C947D58F2D34B9C	FASTA	497	56,311
	10 20 30 40 50 60 MTDLHPARTR VAPSPTGDPH VGTAYMALFD KAWAQRTGGQ FVLRIEDTDR TRLVADSEDQ 70 80 90 100 110 120 IYQTLEWLGL SPDESPLVGG PYEPYKQSER LDTYKPLVEK LIESGHAYRC WCSQERLKQL 130 140 150 160 170 180 REERAAAKSP ETGYDRMCLG MSKEERAKLP GFTETPVVRM LIPEDVDLEF DDLIRGTVRA 190 200 210 220 230 240 PRPDDQVILK ADGFPTYHMA VVVDDHLMGI DTVVRGEEWI SSTPKHLLLY KWLGWEAPKF 250 260 270 280 290 300 AHMPLLRNTD KSKISKRKNP AARLMWFREQ GYLPEALRNF LQLLAYPTVA EGQEMEDFDS 310 320 330 340 350 360 FVSRFDWGNV STGGPVFDVT KLDWLNGQYI RSLDAEVLTD RVLDYADQMC QARHVLGRDL 370 380 390 400 410 420 TQEDRCVIHA AMPLVRERLT LLSEALPKLA FLLTDDDALV FDEDSVAKLK AGADDIQHAA 430 440 450 460 470 480 VEVLKGLDDF SADAIQAALR ARLCDEMGIK PRLAFAPVRV AVTGSRVSPP LFEAMEILGK 490 ESTLRRMQRF EAEIDQK

References

[1]

"The complete genome sequence of Propionibacterium acnes, a commensal of human skin." Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G. Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017283 Genomic DNA. Translation: AAT83592.1.
RefSeq	YP_056550.1. NC_006085.1.
3D structure databases
ProteinModelPortal	Q6A6M1.
ModBase	Search...
Protein-protein interaction databases
STRING	267747.PPA1869.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAT83592; AAT83592; PPA1869.
GeneID	2933042.
KEGG	pac:PPA1869.
PATRIC	23038549. VBIProAcn64440_1924.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252720.
KO	K01885.
OMA	EEWISST.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	PACN267747:GHO9-1897-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. 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_PROAC

Accession

Primary (citable) accession number: Q6A6M1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	September 13, 2004
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program