Skip Header

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

Glutamate--tRNA ligase

Gene

gltX

Organism
Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So ce56))
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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei319 – 3191ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSCEL448385:GJ75-605-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligase (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
GluRS
Gene namesi
Name:gltX
Ordered Locus Names:sce0573
OrganismiSorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So ce56))
Taxonomic identifieri448385 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesSorangiineaePolyangiaceaeSorangium
ProteomesiUP000002139 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 571571Glutamate--tRNA ligasePRO_0000367769Add
BLAST

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi448385.sce0573.

Structurei

3D structure databases

ProteinModelPortaliA9GVA4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi38 – 4811"HIGH" regionAdd
BLAST
Motifi316 – 3205"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK01885.
OrthoDBiEOG6DRPF7.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
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.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A9GVA4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLFGDAAA SARRPEEYEA RYPRRALPKG AMVTRYAPSP TGFMHIGGIF
60 70 80 90 100
VSLINKRLSL QSEGVFYLRL EDTDVKRAIP GALDTIVDSL ARFDLSPQEG
110 120 130 140 150
VLRAPAKDGD ASSRGEFVQQ GSYGPYIQTE RVEIYRDYAI DLIRRGFAYP
160 170 180 190 200
CFCTVEELDA IRQEQMALTV KPGVHGRWAK WRDAPLARVK EALAGGTPFV
210 220 230 240 250
LRLRAPDDVS GRVEWKDGVK GVISMPVNDL DTILLKSDGI PTYHFAHAID
260 270 280 290 300
DHLMRTTHVI RGDEWISSMP LHLQLFRTLG FRPVEYAHVP PIQKLDRVEE
310 320 330 340 350
VDPETGETKV SDARRKLSKR KDPEANIAYY REIGVPETGT IEYLLNIANS
360 370 380 390 400
AFEDWRKANP DKPYSAFPLK LNKLAPGGAL SDMVKLKSVS QAVVSRMSAE
410 420 430 440 450
DVYAQGLDWA REHDKELAAL MERDPEYTKR ALGIERGGKK SNKRITTWPD
460 470 480 490 500
LRPQLFFFYD ELYDRVDALD FPENVPEGDR QPLLRQMLDT FDPADSKEAW
510 520 530 540 550
FEKIRQIAVA SGYAGEVKQY KASPESWKGH VGDVSMLLRV AVCGTRNSPD
560 570
LTEVMAVLGE PRVRARIARF L
Length:571
Mass (Da):64,413
Last modified:March 24, 2009 - v2
Checksum:i73C98C4BCF1C7DD5
GO

Sequence cautioni

The sequence CAN90730.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM746676 Genomic DNA. Translation: CAN90730.1. Different initiation.
RefSeqiWP_012233208.1. NC_010162.1.
YP_001611210.1. NC_010162.1.

Genome annotation databases

EnsemblBacteriaiCAN90730; CAN90730; sce0573.
KEGGiscl:sce0573.
PATRICi23658789. VBISorCel80414_0623.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM746676 Genomic DNA. Translation: CAN90730.1. Different initiation.
RefSeqiWP_012233208.1. NC_010162.1.
YP_001611210.1. NC_010162.1.

3D structure databases

ProteinModelPortaliA9GVA4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi448385.sce0573.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAN90730; CAN90730; sce0573.
KEGGiscl:sce0573.
PATRICi23658789. VBISorCel80414_0623.

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK01885.
OrthoDBiEOG6DRPF7.

Enzyme and pathway databases

BioCyciSCEL448385:GJ75-605-MONOMER.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
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.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of the myxobacterium Sorangium cellulosum."
    Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O., Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J., Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.
    , Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C., Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T., Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S., Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F., Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G., Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D., Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H., Puehler A., Mueller R.
    Nat. Biotechnol. 25:1281-1289(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: So ce56.

Entry informationi

Entry nameiSYE_SORC5
AccessioniPrimary (citable) accession number: A9GVA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: June 24, 2015
This is version 46 of the entry and version 2 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.