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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Symbiobacterium thermophilum (strain T / IAM 14863)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).UniRule annotation

Catalytic activityi

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi106 – 1061ZincUniRule annotation
Metal bindingi108 – 1081ZincUniRule annotation
Metal bindingi133 – 1331ZincUniRule annotation
Metal bindingi135 – 1351ZincUniRule annotation
Binding sitei253 – 2531ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW
  4. tRNA binding Source: InterPro

GO - Biological processi

  1. glutamyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciSTHE292459:GJMM-17-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligaseUniRule annotation (EC:6.1.1.17UniRule annotation)
Alternative name(s):
Glutamyl-tRNA synthetaseUniRule annotation
Short name:
GluRSUniRule annotation
Gene namesi
Name:gltXUniRule annotation
Ordered Locus Names:STH16
OrganismiSymbiobacterium thermophilum (strain T / IAM 14863)
Taxonomic identifieri292459 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesSymbiobacteriaceaeSymbiobacterium
ProteomesiUP000000417 Componenti: Chromosome

Subcellular locationi

  1. Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482Glutamate--tRNA ligasePRO_0000119673Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi292459.STH16.

Structurei

3D structure databases

ProteinModelPortaliQ67TJ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi9 – 1911"HIGH" regionAdd
BLAST
Motifi250 – 2545"KMSKS" region

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK09698.
OMAiAFRCFCT.
OrthoDBiEOG6DRPF7.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q67TJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVRVRIAPS PTGPIHVGNV HTALFNWLFA RHHGGKFILR FEDTDLERSR
60 70 80 90 100
PEWEQVIFED LKWLGIDWDE GPDIGGPYGP YRQTERLDLY RKYAQQLLES
110 120 130 140 150
GHVYKCYCTK EEEDADRREA QAAGRPYQYK GRCRDLTPEQ QAAFEAEGRK
160 170 180 190 200
PVLRFRVPRG EVIRFNDLVR GPIEVPTDSI GDFIIMRANG MPLYNFAVVV
210 220 230 240 250
DDVTMNITHV LRGEGHIPNT PVQILIYQAL GFPVPEFGHL GHMTNPERGK
260 270 280 290 300
LSKRKGEAAI RDYREQGYLP EAMLNFMSLL GWTPPGAESG REFLTKEELI
310 320 330 340 350
REFDLSRVTK ASSVFDRNKL NWMNGVYIRK KSLEEFAELA LPFVVSAGLC
360 370 380 390 400
TEEQARARWD WFKEVMAQVH ERVETLAEIP QHVDIFLKDE IEMDEKAARK
410 420 430 440 450
FLTEAVKPFF QRVSEGLRSV EWSVPAIEQL VRSIQEEMGL TPKESFQPIR
460 470 480
VAITGRTASP GLFETIYLIG RERVLERMAP YC
Length:482
Mass (Da):55,490
Last modified:October 11, 2004 - v1
Checksum:iEEC40EB190A7FBFD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006840 Genomic DNA. Translation: BAD39001.1.
RefSeqiYP_073845.1. NC_006177.1.

Genome annotation databases

EnsemblBacteriaiBAD39001; BAD39001; STH16.
KEGGisth:STH16.
PATRICi23778064. VBISymThe116959_0018.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006840 Genomic DNA. Translation: BAD39001.1.
RefSeqiYP_073845.1. NC_006177.1.

3D structure databases

ProteinModelPortaliQ67TJ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi292459.STH16.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD39001; BAD39001; STH16.
KEGGisth:STH16.
PATRICi23778064. VBISymThe116959_0018.

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK09698.
OMAiAFRCFCT.
OrthoDBiEOG6DRPF7.

Enzyme and pathway databases

BioCyciSTHE292459:GJMM-17-MONOMER.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
    Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
    Nucleic Acids Res. 32:4937-4944(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: T / IAM 14863.

Entry informationi

Entry nameiSYE_SYMTH
AccessioniPrimary (citable) accession number: Q67TJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 11, 2004
Last modified: April 29, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.