Q1Q845 (SYE_PSYCK) 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:	Pcryo_2381

Organism

Psychrobacter cryohalolentis (strain K5) [Complete proteome] [HAMAP]

Taxonomic identifier

335284 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Psychrobacter

Protein attributes

Sequence length	509 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 – 509	509	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_1000001943
Regions
	Motif	20 – 30	11	"HIGH" region HAMAP MF_00022_B
	Motif	261 – 265	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Metal binding	117	1	Zinc By similarity
	Metal binding	119	1	Zinc By similarity
	Metal binding	144	1	Zinc By similarity
	Metal binding	146	1	Zinc By similarity
	Binding site	264	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1Q845 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: C5D4C77FD311B544	FASTA	509	57,493
	10 20 30 40 50 60 MMQPSTSTNS IRPVRTRIAP SPTGFPHVGT AYIALFNLAF AKAHGGEFIL RIEDTDQTRS 70 80 90 100 110 120 TEQSEKMILD ALRWVGLDWA EGPDIGGPHA PYRQSERSDI YKKHAEQLIE NDHAFRCFCS 130 140 150 160 170 180 SEELDAMRAE QMANGETPRY DGRCAHLAAE KTEQLVAEGK PHVIRMRVPT EGVCQVQDML 190 200 210 220 230 240 RGTVEIPWTQ VDMQVLLKTD GMPTYHLANV VDDHLMDISH VMRGEEWLNS APKHQLLYEY 250 260 270 280 290 300 FGWEMPVLCH MPLLRNPDKS KLSKRKNPTS ITYYRDAGVL PEALLNYLGR MGYSMPDEAE 310 320 330 340 350 360 QFTLEEMIAS FDIQRVSLGG PIFDIEKLNW LNSEWLRALT PEELKNKILE WASNSDKLTA 370 380 390 400 410 420 IAAAIQPRIE LLSDAVNWSG FYFQNLPDIN AESFTHKSLT PEQIMDMLQL SLWQLEVLPT 430 440 450 460 470 480 WSEENIYATL KGLAAHLDIK MRDFMAPFFI AIAGSTSSTP VMNSMAIIGA DMTLTRLRHA 490 500 VDVLGGLGKK KLKKLEKQAA ELPDFLAAE

References

[1]

"Complete sequence of chromosome of Psychrobacter cryohalolentis K5." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K5.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000323 Genomic DNA. Translation: ABE76158.1.
RefSeq	YP_581642.1. NC_007969.1.
3D structure databases
ProteinModelPortal	Q1Q845.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1Q845.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4034355.
GenomeReviews	Gene locus Pcryo_2381 in contig CP000323_GR.
KEGG	pcr:Pcryo_2381.
NMPDR	fig|335284.3.peg.1816.
PATRIC	23064415. VBIPsyCry128170_2514.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	DKETAND.
PhylomeDB	Q1Q845.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	PCRY335284:PCRYO_2381-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_PSYCK

Accession

Primary (citable) accession number: Q1Q845

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 16, 2006
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program