Q6MEN1 (SYE_PARUW) 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:	pc0244

Organism

Protochlamydia amoebophila (strain UWE25) [Complete proteome] [HAMAP]

Taxonomic identifier

264201 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Parachlamydiaceae › Candidatus Protochlamydia

Protein attributes

Sequence length	502 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 – 502	502	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000119618
Regions
	Motif	9 – 19	11	"HIGH" region HAMAP MF_00022_B
	Motif	250 – 254	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Metal binding	106	1	Zinc By similarity
	Metal binding	108	1	Zinc By similarity
	Metal binding	133	1	Zinc By similarity
	Metal binding	135	1	Zinc By similarity
	Binding site	253	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6MEN1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 1903CD607A03A1A2	FASTA	502	58,420
	10 20 30 40 50 60 MSVRVRIAPS PTGDPHVGTA YMALFNMIFA RHYNGTFILR IEDTDRARSR PEYEENIYSA 70 80 90 100 110 120 LKWANIQWDE GPDIGGAYGP YRQSERFDIY KQYAEELLSK GKAYKCFCTA AELDEMRELS 130 140 150 160 170 180 AKQGGRQGYD RRCRHLTPDE IIEREQAELS YVIRLKVPLN GECVYEDAIK KRMTFPWADI 190 200 210 220 230 240 DDQVLLKSDG FPTYHLANVV DDYLMKISHV IRGDEWMSST PKHILLYESF GWTPPTFLHM 250 260 270 280 290 300 PLLLGKDGKK LSKRKNPTSI FFYRDSGYLS EAFINFLTLM GYSMTGDQEI YSLDDIIREF 310 320 330 340 350 360 DYKRIGVSGA IFDVQKLDWV NQQYLIKNIP VEQLWDRIKE WSFNDEFMQR LMPLCHSRIK 370 380 390 400 410 420 TFGDFMDLFN FLFINHLHYN DAIFVVKDLS KEQICYLIQS LIWRLDELEN WNGTGVNQAS 430 440 450 460 470 480 REIAEIFGVN HKKIVMPILF ASLMSKTQGP PLFDSVNLLG KDRTRARLLK AMEYLGGISN 490 500 KKMASLKKAW QEKSGQPLMI KD

References

[1]

"Illuminating the evolutionary history of chlamydiae." Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T., Mewes H.-W., Wagner M. Science 304:728-730(2004) [PubMed: 15073324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UWE25.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX908798 Genomic DNA. Translation: CAF22968.1.
RefSeq	YP_007243.1. NC_005861.1.
3D structure databases
ProteinModelPortal	Q6MEN1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6MEN1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2781428.
GenomeReviews	Gene locus pc0244 in contig BX908798_GR.
KEGG	pcu:pc0244.
NMPDR	fig|264201.1.peg.244.
PATRIC	31995772. VBICanPro72727_0246.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	DKETAND.
PhylomeDB	Q6MEN1.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	CPRO264201:PC0244-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_PARUW

Accession

Primary (citable) accession number: Q6MEN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program