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B2HIH4 (SYE_MYCMM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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:MMAR_1719
OrganismMycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP]
Taxonomic identifier216594 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length489 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 – 489489Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367715

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif256 – 2605"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2591ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2HIH4 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 94C9207AEFE1FC89

FASTA48953,715
        10         20         30         40         50         60 
MTSSSVRVRF CPSPTGIPHV GMVRTALFNW AYARHTGGTF VFRIEDTDAA RDSEESYLAL 

        70         80         90        100        110        120 
LDALRWLGLD WDEGPEVDGP YGPYRQSQRT EIYHDVVAKL LTAGEAYYAF STPEEVEARH 

       130        140        150        160        170        180 
IAAGRNPKLG YDNFDRQLTD SQRAAYLAEG RKPVVRLRMP DTDLAWHDLV RGPTTFAAGS 

       190        200        210        220        230        240 
VPDFALTRAT GDPLYTLVNP CDDALMKITH VLRGEDLLPS TPRQIALYQA LMRIGIAERV 

       250        260        270        280        290        300 
PEFAHLPTVL GEGTKKLSKR DPQSNLFAHR DRGFIPEGLL NYLALLGWAI ADDHDLFSLD 

       310        320        330        340        350        360 
EMVAAFDVAD VNSNPARFDQ KKADAINAEH IRMLDVADFT ARLRAYLDTH GHQLALDDAA 

       370        380        390        400        410        420 
FAVAAELVQT RIVVLEDAWA LLKFLNDDRY AIDPKAAAKE LGPDAGPVLD AAIAALDGAA 

       430        440        450        460        470        480 
DWTTADIEAA LKTALIEGMA LKPRKAFGPI RVAATGTTVS PPLFESLELL GRERSLGRLR 


SARDQVGSP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000854 Genomic DNA. Translation: ACC40168.1.
RefSeqYP_001850023.1. NC_010612.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216594.MMAR_1719.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACC40168; ACC40168; MMAR_1719.
GeneID6225976.
KEGGmmi:MMAR_1719.
PATRIC18064305. VBIMycMar75906_1839.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycMMAR216594:GJOB-1727-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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_MYCMM
AccessionPrimary (citable) accession number: B2HIH4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: February 19, 2014
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

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries