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Q8XBN2

- SYE_ECO57

UniProt

Q8XBN2 - SYE_ECO57

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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Escherichia coli O157:H7
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

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

BioCyciECOL386585:GJFA-3234-MONOMER.
ECOO157:GLTX-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:Z3665, ECs3278
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: 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_0000119556Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi155864.Z3665.

Structurei

3D structure databases

ProteinModelPortaliQ8XBN2.
SMRiQ8XBN2. Positions 2-468.
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.

Q8XBN2 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKIKTRFAPS PTGYLHVGGA RTALYSWLFA RNHGGEFVLR IEDTDLERST
60 70 80 90 100
PEAIEAIMDG MNWLSLEWDE GPYFQTKRFD 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 LAFIAERENQ Q
Length:471
Mass (Da):53,756
Last modified:March 1, 2002 - v1
Checksum:iFC5A227F3CEF2592
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG57524.1.
BA000007 Genomic DNA. Translation: BAB36701.1.
PIRiF91038.
H85882.
RefSeqiNP_288968.1. NC_002655.2.
NP_311305.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG57524; AAG57524; Z3665.
BAB36701; BAB36701; BAB36701.
GeneIDi915601.
957612.
KEGGiece:Z3665.
ecs:ECs3278.
PATRICi18355960. VBIEscCol44059_3179.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG57524.1 .
BA000007 Genomic DNA. Translation: BAB36701.1 .
PIRi F91038.
H85882.
RefSeqi NP_288968.1. NC_002655.2.
NP_311305.1. NC_002695.1.

3D structure databases

ProteinModelPortali Q8XBN2.
SMRi Q8XBN2. Positions 2-468.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 155864.Z3665.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG57524 ; AAG57524 ; Z3665 .
BAB36701 ; BAB36701 ; BAB36701 .
GeneIDi 915601.
957612.
KEGGi ece:Z3665.
ecs:ECs3278.
PATRICi 18355960. VBIEscCol44059_3179.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci ECOL386585:GJFA-3234-MONOMER.
ECOO157:GLTX-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiSYE_ECO57
AccessioniPrimary (citable) accession number: Q8XBN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: March 1, 2002
Last modified: October 29, 2014
This is version 81 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