Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q67TJ2

- SYE_SYMTH

UniProt

Q67TJ2 - SYE_SYMTH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Symbiobacterium thermophilum (strain T / IAM 14863)
Status
Reviewed - 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 lineageiBacteriaFirmicutesClostridiaClostridialesClostridiales Family XVIII. Incertae SedisSymbiobacterium
ProteomesiUP000000417: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
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.
OMAiVTGQTHG.
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.
GeneIDi2980022.
KEGGisth:STH16.
PATRICi23778064. VBISymThe116959_0018.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006840 Genomic DNA. Translation: BAD39001.1 .
RefSeqi YP_073845.1. NC_006177.1.

3D structure databases

ProteinModelPortali Q67TJ2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 292459.STH16.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD39001 ; BAD39001 ; STH16 .
GeneIDi 2980022.
KEGGi sth:STH16.
PATRICi 23778064. VBISymThe116959_0018.

Phylogenomic databases

eggNOGi COG0008.
HOGENOMi HOG000252720.
KOi K09698.
OMAi VTGQTHG.
OrthoDBi EOG6DRPF7.

Enzyme and pathway databases

BioCyci STHE292459:GJMM-17-MONOMER.

Family and domain databases

Gene3Di 1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPi MF_00022_B. Glu_tRNA_synth_B.
InterProi IPR008925. 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 ]
PANTHERi PTHR10119. PTHR10119. 1 hit.
Pfami PF00749. tRNA-synt_1c. 1 hit.
[Graphical view ]
PRINTSi PR00987. TRNASYNTHGLU.
SUPFAMi SSF48163. SSF48163. 1 hit.
TIGRFAMsi TIGR00464. gltX_bact. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 73 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