O67271 (SYE_AQUAE) 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:	aq_1221

Organism

Aquifex aeolicus (strain VF5)

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	473 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 – 473	473	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000119495
Regions
	Motif	10 – 20	11	"HIGH" region HAMAP MF_00022_B
	Motif	242 – 246	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Metal binding	98	1	Zinc By similarity
	Metal binding	100	1	Zinc By similarity
	Metal binding	125	1	Zinc By similarity
	Metal binding	127	1	Zinc By similarity
	Binding site	245	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	O67271 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 5CB4D1590973E07A	FASTA	473	55,122
	10 20 30 40 50 60 MSKVKTRFAP SPTGYLHLGN ARTAIFSYLF ARHNNGGFVL RIEDTDPERS KKEYEEMLIE 70 80 90 100 110 120 DLKWLGIDWD EFYRQSERFD IYREYVNKLL ESGHAYPCFC TPEELEKERE EARKKGIPYR 130 140 150 160 170 180 YSGKCRHLTP EEVEKFKKEG KPFAIRFKVP ENRTVVFEDL IKGHIAINTD DFGDFVIVRS 190 200 210 220 230 240 DGSPTYNFVV VVDDALMGIT HVIRGEDHIP NTPKQILIYE ALGFPVPKFA HLPVILGEDR 250 260 270 280 290 300 SKLSKRHGAV SVRAYREEGY MPEALFNYLC LLGWSPPEEG REIFSKEELI KIFDLKDVND 310 320 330 340 350 360 SPAVFNKEKL KWMNGVYIRE VLPLDVLLER AIPFLEKAGY DTSDREYIKK VLEYTRDSFD 370 380 390 400 410 420 TLSEMVDRLR PFFVDEFEIP EELWSFLDDE KAYQVLSAFL EKIREKKPET PQEVKKLAKE 430 440 450 460 470 IQKALKVKPP QVWKPLRIAL TGELEGVGID ILIAVLPKEK IEKRILRVLE KLS

References

[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000657 Genomic DNA. Translation: AAC07230.1.
PIR	D70405.
RefSeq	NP_213835.1. NC_000918.1.
3D structure databases
ProteinModelPortal	O67271.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1192617.
GenomeReviews	Gene locus aq_1221 in contig AE000657_GR.
KEGG	aae:aq_1221.
NMPDR	fig|224324.1.peg.850.
PATRIC	20959662. VBIAquAeo85532_0950.
Phylogenomic databases
HOGENOM	HBG628189.
OMA	ANFNDES.
PhylomeDB	O67271.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	AAEO224324:AQ_1221-MONOMER.
Family and domain databases
HAMAP	MF_00022_B. Glu_tRNA_synth_B. [Tree]
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR020752. aa-tRNA-synth_I_codon-bd_sub1. 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:1.10.8.70. aa-tRNA-synth_I_codon-bd_sub1. 1 hit. 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_AQUAE

Accession

Primary (citable) accession number: O67271

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program