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Reviewed, UniProtKB/Swiss-Prot B5EMF9 (SYE1_ACIF5)

Last modified February 9, 2010. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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
Ordered Locus Names: Lferr_0584
OrganismAcidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum ferrooxidans (ATCC 53993)) [Complete proteome] [HAMAP]
Taxonomic identifier380394 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Acidithiobacillales › Acidithiobacillaceae › Acidithiobacillus

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Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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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

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. HAMAP MF_00022

Subunit structure

Monomer By similarity. HAMAP MF_00022

Subcellular location

Cytoplasm By similarity HAMAP MF_00022.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

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Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP 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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000367597

Regions

Motif9 – 1911"HIGH" region HAMAP MF_00022
Motif236 – 2405"KMSKS" region HAMAP MF_00022

Sites

Metal binding981Zinc By similarity
Metal binding1001Zinc By similarity
Metal binding1251Zinc By similarity
Metal binding1271Zinc By similarity
Binding site2391ATP By similarity

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Sequences

Sequence LengthMass (Da)Tools
B5EMF9-1 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: 08F22AF145DC1554

FASTA46651,975
        10         20         30         40         50         60 
MSVRTRFAPS PTGYLHIGGV RTALYSWLHA RRQGGHFILR IEDTDVERST PEATVAILEG 

        70         80         90        100        110        120 
MAWLGLDWDE GPFYQMRRMD RYREVLAQML AAGTAYHCYC SREEVEAMRE DQRQRGEKPR 

       130        140        150        160        170        180 
YDGRCRERTT VPEGVAPVIR FRSPDDGETV VEDLIHGTVR FQNSEMDDLI IARSDGTPTY 

       190        200        210        220        230        240 
NFCVVVDDWD MGITHVIRGD DHLNNTPRQM QILQALGARV PVYAHVPMIL GPDKQKLSKR 

       250        260        270        280        290        300 
HGAVSVLEYR EQGFLPDALL NFLVRLGWSH GDQEIFTREE MVEFFRIDAV NKAASAFNPE 

       310        320        330        340        350        360 
KLLWINAQHM QRLTPEGLAQ HLLPYLNAVG VTEPLLASGP ELPAVVALLQ ERSKTLVEMA 

       370        380        390        400        410        420 
AAAEMFYVAP VAGEPKDVEK HLHGQSALLA TMTQALGALP NWEAAAIHSV IQELAVTHAD 

       430        440        450        460 
GKMGKVAQPL RVAVAGRAVS PPIDATLALL GKEETLARLR RAAAWI

« Hide

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References

[1]"Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Borole A.P.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001132 Genomic DNA. Translation: ACH82838.1.
RefSeqYP_002219045.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6876546.
GenomeReviewsGene locus Lferr_0584 in contig CP001132_GR.
KEGGafe:Lferr_0584.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMAMAHIPLI.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
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]
Gene3DG3DSA: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.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSYE1_ACIF5
AccessionPrimary (citable) accession number: B5EMF9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 14, 2008
Last modified: February 9, 2010
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents