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A6Q9D4 (SYE2_SULNB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase 2
EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2
Gene names
Name:gltX2
Ordered Locus Names:SUN_1138
OrganismSulfurovum sp. (strain NBC37-1) [Complete proteome] [HAMAP]
Taxonomic identifier387093 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Sulfurovum

Protein attributes

Sequence length428 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.

Subcellular location

Cytoplasm By similarity.

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: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367778

Regions

Motif6 – 1611"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
A6Q9D4 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 57A3F687C6A48033

FASTA42848,962
        10         20         30         40         50         60 
MLRFAPSPTG DMRTEQLRIA IFNYIVAKQK EVNFIVRIED TDKERNITGK DTEILQILEK 

        70         80         90        100        110        120 
FAITHDSVFH QSEHLNIHQT LAIRLLEEGK AFVCTCTPEA PESDKTPSRY NGKCFNVDKE 

       130        140        150        160        170        180 
ELKRLKEEKI PFVIRLKKPE HDMIIHDLYK GETVTSADEV DSFVILRADA TPTENFASAC 

       190        200        210        220        230        240 
DDMLSGIDFI IRSEEHLDET AKQEYVKKQL GYEEETTYAH LPVILNEEGQ KMDEKDDAFT 

       250        260        270        280        290        300 
VKWLFEEGYI PDAIANYLIS LGNTTPTDIF TLPEAIEWFN ITKLSGSPVK FNIEELRLLN 

       310        320        330        340        350        360 
RKHLEKMDDK RLSSLFGFAD ADIGKLAKLY INEAATINEL DARIKAIFSP KDFDGKWGEQ 

       370        380        390        400        410        420 
MRMLEKIIAE APMFATFEAF ESHLMKESGL SGEYFSKPLR VLLTGAEQGP ELSDIYPYIK 


SYLLEVAS

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References

[1]"Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens."
Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K.
Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBC37-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009179 Genomic DNA. Translation: BAF72093.1.
RefSeqYP_001358450.1. NC_009663.1.

3D structure databases

ProteinModelPortalA6Q9D4.
ModBaseSearch...

Protein-protein interaction databases

STRING387093.SUN_1138.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF72093; BAF72093; SUN_1138.
GeneID5362086.
KEGGsun:SUN_1138.
PATRIC23775243. VBISulSp49917_1150.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAFIVRGED.
ProtClustDBPRK12410.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B. Divergent sequence.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR004527. Glu-tRNA-ligase_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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE2_SULNB
AccessionPrimary (citable) accession number: A6Q9D4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: August 21, 2007
Last modified: May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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