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Q9ZFA3 (SYE1_RHOS4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:gluS
Ordered Locus Names:RHOS4_05770
ORF Names:RSP_1995
OrganismRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) [Reference proteome] [HAMAP]
Taxonomic identifier272943 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Protein existenceInferred 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-Rule MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

Sequence similarities

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

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 471471Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000119637

Regions

Motif15 – 2511"HIGH" region HAMAP-Rule MF_00022
Motif243 – 2475"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2461ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZFA3 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 044E8C102AB5FCB9

FASTA47152,136
        10         20         30         40         50         60 
MPAASDKPVV TRFAPSPTGY LHIGGGRTAL FNWLYARGRK GTFLLRIEDT DRERSTPEAT 

        70         80         90        100        110        120 
DAILRGLTWL GLDWDGEVVS QFARKDRHAE VAREMLERGA AYKCFSTQEE IEAFRESARA 

       130        140        150        160        170        180 
EGRSTLFRSP WRDADPTSHP DAPFVIRMKA PRSGETVIED EVQGTVRFQN ETLDDMVVLR 

       190        200        210        220        230        240 
SDGTPTYMLA VVVDDHDMGV THVIRGDDHL NNAARQTMVY EAMGWEVPVW AHIPLIHGPD 

       250        260        270        280        290        300 
GKKLSKRHGA LGVEEYQAMG YPAAGMRNYL ARLGWSHGDD EFFTSEQAMD WFDLGGIGRS 

       310        320        330        340        350        360 
PARLDFKKLE SVCGQHIAVM EDAELMREIA AYLAAARKPA LTDLQAARLE KGLYALKDRA 

       370        380        390        400        410        420 
KTFPELLEKA RFALESRPIV ADDAAAKALD PVSRGILREL TPMLQAASWS KQDLEAILTA 

       430        440        450        460        470 
FASEKGMGFG KLAAPLRTAL AGRTVTPSVY DMMLVIGRDE TIARLEDAAA A 

« Hide

References

« Hide 'large scale' references
[1]"Trp-ing up paradigms: distribution of tryptophan biosynthesis genes in Rhodobacter sphaeroides 2.4.1."
Simmons A.E., Mackenzie R.C., Kaplan S.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF108766 Genomic DNA. Translation: AAD09123.1.
CP000143 Genomic DNA. Translation: ABA78145.1.
PIRT46860.
RefSeqYP_352046.1. NC_007493.2.

3D structure databases

ProteinModelPortalQ9ZFA3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272943.RSP_1995.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA78145; ABA78145; RSP_1995.
GeneID3719328.
KEGGrsp:RSP_1995.
PATRIC23150974. VBIRhoSph57909_0884.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAAMGWEVP.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycRSPH272943:GJAS-596-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_RHOS4
AccessionPrimary (citable) accession number: Q9ZFA3
Secondary accession number(s): Q3J4Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries