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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Proteus mirabilis (strain HI4320)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi99ZincUniRule annotation1
Metal bindingi101ZincUniRule annotation1
Metal bindingi126ZincUniRule annotation1
Metal bindingi128ZincUniRule annotation1
Binding sitei241ATPUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminoacyl-tRNA synthetase, Ligase
Biological processProtein biosynthesis
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciPMIR529507:G1GJY-1890-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:PMI1818
OrganismiProteus mirabilis (strain HI4320)
Taxonomic identifieri529507 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesMorganellaceaeProteus
Proteomesi
  • UP000008319 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000900971 – 472Glutamate--tRNA ligaseAdd BLAST472

Proteomic databases

PRIDEiB4EZQ7

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi529507.PMI1818

Structurei

3D structure databases

ProteinModelPortaliB4EZQ7
SMRiB4EZQ7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi10 – 20"HIGH" regionUniRule annotationAdd BLAST11
Motifi238 – 242"KMSKS" regionUniRule annotation5

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C20 Bacteria
COG0008 LUCA
HOGENOMiHOG000252722
KOiK01885
OMAiHYINTLP
OrthoDBiPOG091H021W

Family and domain databases

CDDicd00808 GluRS_core, 1 hit
Gene3Di1.10.10.350, 1 hit
3.40.50.620, 1 hit
HAMAPiMF_00022 Glu_tRNA_synth_type1, 1 hit
InterProiView protein in InterPro
IPR008925 aa-tRNA-synth_I_codon-bd
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
IPR020058 Glu/Gln-tRNA-synth_Ib_cat-dom
IPR033910 GluRS_core
IPR014729 Rossmann-like_a/b/a_fold
PfamiView protein in Pfam
PF00749 tRNA-synt_1c, 1 hit
PRINTSiPR00987 TRNASYNTHGLU
SUPFAMiSSF48163 SSF48163, 1 hit
TIGRFAMsiTIGR00464 gltX_bact, 1 hit
PROSITEiView protein in PROSITE
PS00178 AA_TRNA_LIGASE_I, 1 hit

Sequencei

Sequence statusi: Complete.

B4EZQ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKIKTRFAP SPTGYLHVGG ARTALYSWLF SRHNKGEFVL RIEDTDLERS
60 70 80 90 100
TQPAIDAIMD GMNWLNLNWD EGPYYQTKRF DRYNQVIDQM LAAGTAYRCY
110 120 130 140 150
CSKERLEKLR EDQMAKGEKP RYDGCCRHGD HNHTPDEPHV VRFLNPQEGS
160 170 180 190 200
VIFNDKIRGP IEFSNQELDD LIIRRTDGSP TYNFCVVIDD WDMEITHVIR
210 220 230 240 250
GEDHINNTPR QINILKALGA PVPEYAHVSM ILGDDGKKLS KRYNAVSVMQ
260 270 280 290 300
YRDDGYLPEA LLNYLVRLGW SHGDQEIFSI DEMIKDFTLE AISKSASAFN
310 320 330 340 350
TDKLLWLNHH YINTLPAEQV AVHLDWHIKQ QNIDTSNGPS LVELIKLLGE
360 370 380 390 400
RCKTLKEMAE SCHYFYVDFD SFEETAAKKH LRPVARQPLE VVRDKLSAIT
410 420 430 440 450
DWTAENVHKA IQETAEELEV GMGKVGMPLR VAVTGAGQSP ALDVTVHAIG
460 470
KARSIARINK ALDFITDREN QA
Length:472
Mass (Da):53,805
Last modified:September 23, 2008 - v1
Checksum:i05D3AC4301973CC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM942759 Genomic DNA Translation: CAR43779.1
RefSeqiWP_012368116.1, NC_010554.1

Genome annotation databases

EnsemblBacteriaiCAR43779; CAR43779; PMI1818
GeneIDi6802956
KEGGipmr:PMI1818
PATRICifig|529507.6.peg.1769

Similar proteinsi

Entry informationi

Entry nameiSYE_PROMH
AccessioniPrimary (citable) accession number: B4EZQ7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: March 28, 2018
This is version 62 of the entry and version 1 of the sequence. See 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

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