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Q3M3H8 (SYE_ANAVT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:Ava_4861
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length481 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
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 – 481481Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237335

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif247 – 2515"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2501ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3M3H8 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 795CAB506936C45C

FASTA48154,272
        10         20         30         40         50         60 
MTVRVRIAPS PTGNLHIGTA RTAVFNWLFA RHHGGTFILR IEDTDLERSR PEYTENIMTG 

        70         80         90        100        110        120 
LRWLGLNWDE GPFFQSQRLD LYQKAVKQLL DQGLAYRCYT TSEELEALRE AQKAKGEAPR 

       130        140        150        160        170        180 
YDNRHRHLTP EQEAEFKAQG RSFVIRFKID DEREIVWNDL VRGKMSWRGS DLGGDMVIAR 

       190        200        210        220        230        240 
ASENDTGQPL YNFVVVIDDI DMQISHVIRG EDHIANTAKQ ILLYEAFGAK IPEFAHTPLI 

       250        260        270        280        290        300 
LNMEGRKLSK RDGVTSISDF QQMGFTSEGL VNYMTLLGWS PPDSTQEIFT LEAAAKEFTF 

       310        320        330        340        350        360 
ERVNKAGAKF DWAKLDWLNS QYIHNTPVDQ LTDLLIPYWE AAGYSFAGGR DRPWLEQLVG 

       370        380        390        400        410        420 
LLSASLTRLT DAVDMSKLFF SETVELSEEG SKQLQQEGSK AVLEAIIAAL EAQTQLTENA 

       430        440        450        460        470        480 
AQDIIKQVVK AQNVKKGLVM RSLRVALTGD VHGPDLIQSW LLLNQIGLDK PRLSQAIAAS 


L 

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References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29413 / PCC 7937.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000117 Genomic DNA. Translation: ABA24458.1.
RefSeqYP_325353.1. NC_007413.1.

3D structure databases

ProteinModelPortalQ3M3H8.
SMRQ3M3H8. Positions 2-477.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING240292.Ava_4861.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA24458; ABA24458; Ava_4861.
GeneID3679281.
KEGGava:Ava_4861.
PATRIC35431235. VBIAnaVar43351_6137.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMADIDMQIS.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycAVAR240292:GCY3-4923-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 nameSYE_ANAVT
AccessionPrimary (citable) accession number: Q3M3H8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: October 25, 2005
Last modified: May 14, 2014
This is version 59 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