Reviewed, UniProtKB/Swiss-Prot Q83EV3 (SYE1_COXBU)

Names and origin

Protein names

Recommended name:
    Glutamyl-tRNA synthetase 1
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase 1
      Short name=GluRS 1

Gene names

Name:	gltX1
Synonyms:	gltX-1
Ordered Locus Names:	CBU_0205

Organism

Coxiella burnetii [Complete proteome] [HAMAP]

Taxonomic identifier

777 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella

Protein attributes

Sequence length	469 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm. HAMAP MF_00022
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: 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 zinc 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 – 469	469	Glutamyl-tRNA synthetase 1 HAMAP MF_00022		PRO_0000119550
Regions
	Motif	10 – 20	11	"HIGH" region HAMAP MF_00022
	Motif	237 – 241	5	"KMSKS" region HAMAP MF_00022
Sites
	Metal binding	99	1	Zinc By similarity
	Metal binding	101	1	Zinc By similarity
	Metal binding	126	1	Zinc By similarity
	Metal binding	128	1	Zinc By similarity
	Binding site	240	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q83EV3-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: E6C2E5C22060D888	FASTA	469	53,697
	10 20 30 40 50 60 MKHIRTRFAP SPTGYLHIGG VRTALFSWLF ARQNNGAFIL RIEDTDVARS TQASVDAILE 70 80 90 100 110 120 GLRWLQIDWN EGPYYQSQRM DRYREVIEQL VKSDDAYRCY CSKERLIELR NTQLKNKQKP 130 140 150 160 170 180 RYDGFCRDKA PRQSNEPFVI RFRNPVEGAV VFDDLIRGTI SIDNRELDDL IIARSDGGPT 190 200 210 220 230 240 YNLTVVVDDW DMKITHVIRG DDHINNTPRQ INILHALGAE LPHYGHVPMI LGPDGKRLSK 250 260 270 280 290 300 RHGAVSVLQY RDEGYLPEAL MNYLIRLGWA HGDQEIFSRE EMVQLFDISA VSRSPAAFNP 310 320 330 340 350 360 EKLLWLNQHY LKTVSPTIIA EAFATQLEKA GTDLRNGPSL EQVIALQAER TKTLKEMAQR 370 380 390 400 410 420 SLYFYQEVRS YDEKAARKHL LATIVEPLQR VRERLASLPS WEKEAIHEVI VETAQLHQLK 430 440 450 460 LGQLAQPIRV ALTGDTVSPP IDATLYLIGR DSALKRLDHA IRFIHQGMG

References

[1]

"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed: 12704232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nine Mile phase I / RSA 493.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016828 Genomic DNA. Translation: AAO89765.2. Different initiation.
RefSeq	NP_819251.2.
3D structure databases
HSSP	HSSP built from PDB template 1J09 based on UniProtKB P27000.
ModBase	Search...
Genome annotation databases
GeneID	1208081.
GenomeReviews	Gene locus CBU_0205 in contig AE016828_GR.
KEGG	cbu:CBU_0205.
NMPDR	fig|227377.1.peg.195.
TIGR	CBU_0205.
Phylogenomic databases
HOGENOM	Q83EV3.
OMA	MAHIPLI.
Enzyme and pathway databases
BioCyc	CBUR227377:CBU_0205-MON.
BRENDA	6.1.1.17. 256353.
Family and domain databases
HAMAP	MF_00022. [Tree]
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR001412. aa-tRNA-synth_I_CS. IPR004527. Glu-tRNA-synth_Ic_bac/mito. IPR000924. Glu/Gln-tRNA-synth_Ic. IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl. IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom. IPR020060. Glu/Gln-tRNA-synth_Ic_N. 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. 1 hit. G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 1 hit.
Pfam	PF00749. tRNA-synt_1c. 1 hit. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
TIGRFAMs	TIGR00464. gltX_bact. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYE1_COXBU

Accession

Primary (citable) accession number: Q83EV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)