Q60BG7 (SYE1_METCA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase 1
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1

Gene names

Name:	gltX1
Synonyms:	gltX-1
Ordered Locus Names:	MCA0510

Organism

Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) [Complete proteome] [HAMAP]

Taxonomic identifier

243233 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Methylococcales › Methylococcaceae › Methylococcus

Protein attributes

Sequence length	466 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 – 466	466	Glutamate--tRNA ligase 1 HAMAP MF_00022_B		PRO_0000119597
Regions
	Motif	10 – 20	11	"HIGH" region HAMAP MF_00022_B
	Motif	247 – 251	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Metal binding	103	1	Zinc By similarity
	Metal binding	105	1	Zinc By similarity
	Metal binding	130	1	Zinc By similarity
	Metal binding	132	1	Zinc By similarity
	Binding site	250	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q60BG7 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: ABF0C016F522C4D1	FASTA	466	52,121
	10 20 30 40 50 60 MSAIKTRFAP SPTGLIHLGN ARTALFSALG GDVFVLRIED TDLERSRAEF VAELMNDLRW 70 80 90 100 110 120 LGLDWQEGPR GAEPDPDWYQ SRRGEIYATY YRLLEEKGLA YPCFCTPLEL EVSRKVQLGS 130 140 150 160 170 180 GRPPRYSGRC AHLPADEVRR RHEEGLAATL RFRVPKDRVV EFEDEVRGPQ RFAGEDIGDF 190 200 210 220 230 240 IIRRADGSPA FFFCNAIDDA LMGITRVLRG EDHLANTPRQ LMILAALDLP RPRYAHISLI 250 260 270 280 290 300 VGDDGAPLSK RNGSRSIKQL REEGYFPEAV VNMLARLGHH YDSAELLGLP ALRAGFDIRR 310 320 330 340 350 360 LGRSPARFDV SHLDHWQGLA VRGAADDTLW HWLHTETRAV VPDAHRAGFL DLVRSNCLFP 370 380 390 400 410 420 KEADAWARIL FTDELELAAD IAAVAQAAGE AFYLAAIDAA TESPDDFAAF LAGLKRRSGA 430 440 450 460 KGKHLFLPLR AALTGSLDGP ELAKIYQMLD KPRLHRRLAE FTYESE

References

[1]

"Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath)." Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S., Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E., Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J. , Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L., Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H., Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R., Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A. PLoS Biol. 2:1616-1628(2004) [PubMed: 15383840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33009 / NCIMB 11132 / Bath.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017282 Genomic DNA. Translation: AAU93301.1.
RefSeq	YP_113029.1. NC_002977.6.
3D structure databases
ProteinModelPortal	Q60BG7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3103869.
GenomeReviews	Gene locus MCA0510 in contig AE017282_GR.
KEGG	mca:MCA0510.
NMPDR	fig|243233.4.peg.993.
PATRIC	22604770. VBIMetCap22254_0521.
TIGR	MCA0510.
Phylogenomic databases
HOGENOM	HBG628189.
OMA	WQEGPEV.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	MCAP243233:MCA_0510-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

SYE1_METCA

Accession

Primary (citable) accession number: Q60BG7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	November 23, 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