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 1

Gene

gltX1

Organism
Helicobacter pylori (strain G27)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei241ATPUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciHPYL563041:G1GTQ-465-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligase 1UniRule annotation (EC:6.1.1.17UniRule annotation)
Alternative name(s):
Glutamyl-tRNA synthetase 1UniRule annotation
Short name:
GluRS 1UniRule annotation
Gene namesi
Name:gltX1UniRule annotation
Ordered Locus Names:HPG27_434
OrganismiHelicobacter pylori (strain G27)
Taxonomic identifieri563041 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
Proteomesi
  • UP000001735 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003676811 – 463Glutamate--tRNA ligase 1Add BLAST463

Proteomic databases

PRIDEiB5Z6J9

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

Secondary structure

1463
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Helixi18 – 33Combined sources16
Beta strandi37 – 42Combined sources6
Helixi49 – 65Combined sources17
Beta strandi74 – 76Combined sources3
Helixi77 – 79Combined sources3
Helixi80 – 92Combined sources13
Beta strandi95 – 99Combined sources5
Helixi103 – 110Combined sources8
Beta strandi140 – 143Combined sources4
Beta strandi150 – 155Combined sources6
Turni156 – 158Combined sources3
Beta strandi159 – 164Combined sources6
Helixi165 – 167Combined sources3
Beta strandi172 – 174Combined sources3
Helixi182 – 192Combined sources11
Beta strandi197 – 201Combined sources5
Helixi202 – 205Combined sources4
Helixi207 – 217Combined sources11
Beta strandi224 – 228Combined sources5
Turni241 – 243Combined sources3
Helixi248 – 254Combined sources7
Helixi258 – 266Combined sources9
Beta strandi268 – 270Combined sources3
Beta strandi272 – 274Combined sources3
Helixi280 – 286Combined sources7
Helixi289 – 291Combined sources3
Helixi301 – 313Combined sources13
Helixi318 – 323Combined sources6
Turni325 – 327Combined sources3
Helixi342 – 348Combined sources7
Helixi354 – 365Combined sources12
Helixi373 – 376Combined sources4
Helixi381 – 397Combined sources17
Helixi421 – 432Combined sources12
Beta strandi435 – 437Combined sources3
Helixi441 – 447Combined sources7
Helixi450 – 461Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6B1PX-ray2.50A1-463[»]
ProteinModelPortaliB5Z6J9
SMRiB5Z6J9
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

HOGENOMiHOG000252722
KOiK01885
OMAiAYYAFDT
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.

B5Z6J9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLIVTRFAP SPTGYLHIGG LRTAIFNYLF ARANQGKFFL RIEDTDLSRN
60 70 80 90 100
SIEAANAIIE AFKWVGLEYD GEILYQSKRF EIYKEYIQKL LDEDKAYYCY
110 120 130 140 150
MSKDELDALR EEQKARKETP RYDNRYRDFK GTPPKGIEPV VRIKVPQNEV
160 170 180 190 200
IGFNDGVKGE VKVNTNELDD FIIARSDGTP TYNFVVIVDD ALMGITDVIR
210 220 230 240 250
GDDHLSNTPK QIVLYKALNF KIPNFFHVPM ILNEEGQKLS KRHGATNVMD
260 270 280 290 300
YQEMGYLKEA LVNFLVRLGW SYQDKEIFSM QELLECFDPK DLNSSPSCFS
310 320 330 340 350
WHKLNWLNAH YLKNQSAQKL LELLKPFSFS DLSHLNPAQL DRLLDALKER
360 370 380 390 400
SQTLKELALK IDEVLIAPVE YEEKVFKKLN QALIMPLLEK FKLELKEANF
410 420 430 440 450
NDESALENAM HKIIEEEKIK AGSFMQPLRL ALLGKGGGIG LKEALFILGK
460
TESVKRIENF LKN
Length:463
Mass (Da):53,318
Last modified:November 25, 2008 - v1
Checksum:i4698E5559F338919
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001173 Genomic DNA Translation: ACI27198.1
RefSeqiWP_000053235.1, NC_011333.1

Genome annotation databases

EnsemblBacteriaiACI27198; ACI27198; HPG27_434
KEGGihpg:HPG27_434

Similar proteinsi

Entry informationi

Entry nameiSYE1_HELPG
AccessioniPrimary (citable) accession number: B5Z6J9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: May 23, 2018
This is version 64 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

3D-structure, Complete proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health