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A8A2Q2

- SYE_ECOHS

UniProt

A8A2Q2 - SYE_ECOHS

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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Escherichia coli O9:H4 (strain HS)
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 bindingi98 – 981ZincUniRule annotation
Metal bindingi100 – 1001ZincUniRule annotation
Metal bindingi125 – 1251ZincUniRule annotation
Metal bindingi127 – 1271ZincUniRule annotation
Binding sitei240 – 2401ATPUniRule 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

BioCyciECOL331112:GHHI-2521-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:EcHS_A2537
OrganismiEscherichia coli O9:H4 (strain HS)
Taxonomic identifieri331112 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001123: 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 – 471471Glutamate--tRNA ligasePRO_1000057193Add
BLAST

Proteomic databases

PRIDEiA8A2Q2.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi331112.EcHS_A2537.

Structurei

3D structure databases

ProteinModelPortaliA8A2Q2.
SMRiA8A2Q2. Positions 3-441.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi9 – 1911"HIGH" regionAdd
BLAST
Motifi237 – 2415"KMSKS" region

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252722.
KOiK01885.
OMAiDSHEHHA.
OrthoDBiEOG6DRPF7.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. 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.
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.

A8A2Q2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKIKTRFAPS PTGYLHVGGA RTALYSWLFA RNHGGEFVLR IEDTDLERST
60 70 80 90 100
PEAIEAIMDG MNWLSLEWDE GPYYQTKRFD RYNAVIDQML EEGTAYKCYC
110 120 130 140 150
SKERLEALRE EQMAKGEKPR YDGRCRHSHE HHADDEPCVV RFANPQEGSV
160 170 180 190 200
VFDDQIRGPI EFSNQELDDL IIRRTDGSPT YNFCVVVDDW DMEITHVIRG
210 220 230 240 250
EDHINNTPRQ INILKALKAP VPVYAHVSMI NGDDGKKLSK RHGAVSVMQY
260 270 280 290 300
RDDGYLPEAL LNYLVRLGWS HGDQEIFTRE EMIKYFTLNA VSKSASAFNT
310 320 330 340 350
DKLLWLNHHY INALPPEYVA THLQWHIEQE NIDTRNGPQL ADLVKLLGER
360 370 380 390 400
CKTLKEMAQS CRYFYEDFAE FDADAAKKHL RPVARQPLEV VRDKLAAITD
410 420 430 440 450
WTAENVHHAI QATADELEVG MGKVGMPLRV AVTGAGQSPA LDVTVHAIGK
460 470
TRSIERINKA LDFIAERENQ Q
Length:471
Mass (Da):53,816
Last modified:October 23, 2007 - v1
Checksum:i8264A799E5383398
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000802 Genomic DNA. Translation: ABV06806.1.
RefSeqiYP_001459189.1. NC_009800.1.

Genome annotation databases

EnsemblBacteriaiABV06806; ABV06806; EcHS_A2537.
GeneIDi5594442.
KEGGiecx:EcHS_A2537.
PATRICi18315050. VBIEscCol77814_2484.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000802 Genomic DNA. Translation: ABV06806.1 .
RefSeqi YP_001459189.1. NC_009800.1.

3D structure databases

ProteinModelPortali A8A2Q2.
SMRi A8A2Q2. Positions 3-441.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 331112.EcHS_A2537.

Chemistry

BindingDBi A8A2Q2.

Proteomic databases

PRIDEi A8A2Q2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV06806 ; ABV06806 ; EcHS_A2537 .
GeneIDi 5594442.
KEGGi ecx:EcHS_A2537.
PATRICi 18315050. VBIEscCol77814_2484.

Phylogenomic databases

eggNOGi COG0008.
HOGENOMi HOG000252722.
KOi K01885.
OMAi DSHEHHA.
OrthoDBi EOG6DRPF7.

Enzyme and pathway databases

BioCyci ECOL331112:GHHI-2521-MONOMER.

Family and domain databases

Gene3Di 1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPi MF_00022_B. Glu_tRNA_synth_B.
InterProi 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.
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. "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
    Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
    J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HS.

Entry informationi

Entry nameiSYE_ECOHS
AccessioniPrimary (citable) accession number: A8A2Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: November 26, 2014
This is version 51 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

Documents

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

External Data

Dasty 3