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Q8L1E5

- SYE_SYNE7

UniProt

Q8L1E5 - SYE_SYNE7

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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
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 sitei251 – 2511ATPUniRule 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

BioCyciSYNEL:SYNPCC7942_2393-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:Synpcc7942_2393
OrganismiSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Taxonomic identifieri1140 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000002717: 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 – 481481Glutamate--tRNA ligasePRO_0000119677Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi1140.Synpcc7942_2393.

Structurei

3D structure databases

ProteinModelPortaliQ8L1E5.
SMRiQ8L1E5. Positions 2-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi9 – 1911"HIGH" regionAdd
BLAST
Motifi248 – 2525"KMSKS" region

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252722.
KOiK01885.
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.

Q8L1E5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVRVRIAPS PTGNLHIGTA RTAVFNWLFA RRHQGQFILR IEDTDLERSR
60 70 80 90 100
SEYTDNILTG LQWLGLNWDE GPFYQTQRLD LYKAAVQQLL DSGKAYRCYC
110 120 130 140 150
TEAELEALRE SQRARNEAPR YDNRHRDLTP EQEAAFQAEG REAVIRFRID
160 170 180 190 200
DDREIAWTDL VRDRVVWKGS DLGGDMVIAR RSPAGTIGQP LYNLAVVVDD
210 220 230 240 250
IDMTISHVIR GEDHIANTAK QILLYEALGA AVPEFAHTPL ILNKEGRKLS
260 270 280 290 300
KRDGVTSISD FQNLGYLPEA IANYMTLLGW SPVEGMDERF SLAEAATVFD
310 320 330 340 350
FDRVNKAGAK FDWDKLNWLN SQVIKEKSAS ELVALLQPFW SKAGVDTAAY
360 370 380 390 400
PAAWLEELAT LLGPSLVTLT DIVGQSQLFF SQGIELQEDA IAQLGQAGSK
410 420 430 440 450
AVLQQILEAL PSEALTLEVA KGLIDQAVKA AGVKKGIGMR SLRAALMGSM
460 470 480
QGPDLLTSWV LLHQAGQAQP RLQAAIAAAQ G
Length:481
Mass (Da):53,200
Last modified:October 1, 2002 - v1
Checksum:i82AC99209A06D033
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ440366 Genomic DNA. Translation: CAD29422.1.
CP000100 Genomic DNA. Translation: ABB58423.1.
RefSeqiYP_401410.1. NC_007604.1.

Genome annotation databases

EnsemblBacteriaiABB58423; ABB58423; Synpcc7942_2393.
GeneIDi3774677.
KEGGisyf:Synpcc7942_2393.
PATRICi23790343. VBISynElo51371_2686.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ440366 Genomic DNA. Translation: CAD29422.1 .
CP000100 Genomic DNA. Translation: ABB58423.1 .
RefSeqi YP_401410.1. NC_007604.1.

3D structure databases

ProteinModelPortali Q8L1E5.
SMRi Q8L1E5. Positions 2-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 1140.Synpcc7942_2393.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB58423 ; ABB58423 ; Synpcc7942_2393 .
GeneIDi 3774677.
KEGGi syf:Synpcc7942_2393.
PATRICi 23790343. VBISynElo51371_2686.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SYNEL:SYNPCC7942_2393-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

« Hide 'large scale' publications
  1. "Expression of the glutamyl-tRNA synthetase gene from the cyanobacterium Synechococcus sp PCC 7942 depends on nitrogen availability and the global regulator NtcA."
    Luque I., Contreras A., Zabulon G., Herrero A., Houmard J.
    Mol. Microbiol. 46:1157-1167(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7942.

Entry informationi

Entry nameiSYE_SYNE7
AccessioniPrimary (citable) accession number: Q8L1E5
Secondary accession number(s): Q31KJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: October 1, 2002
Last modified: October 29, 2014
This is version 76 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, 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