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Q9X172

- SYE1_THEMA

UniProt

Q9X172 - SYE1_THEMA

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Protein

Glutamate--tRNA ligase 1

Gene

gltX1

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 3 out of 5- 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).By similarity

Catalytic activityi

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei253 – 2531ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
  3. 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, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligase 1 (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name:
GluRS 1
Gene namesi
Name:gltX1
Ordered Locus Names:TM_1351
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183: Chromosome

Subcellular locationi

Cytoplasm By similarity

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 – 469469Glutamate--tRNA ligase 1PRO_0000119680Add
BLAST

Proteomic databases

PRIDEiQ9X172.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi243274.TM1351.

Structurei

Secondary structure

1
469
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Helixi16 – 3217Combined sources
Beta strandi35 – 384Combined sources
Helixi48 – 503Combined sources
Helixi51 – 6313Combined sources
Beta strandi68 – 703Combined sources
Turni71 – 733Combined sources
Helixi82 – 854Combined sources
Helixi86 – 9813Combined sources
Beta strandi101 – 1055Combined sources
Turni110 – 1123Combined sources
Helixi113 – 1219Combined sources
Helixi130 – 1334Combined sources
Turni134 – 1363Combined sources
Helixi139 – 1479Combined sources
Beta strandi153 – 1564Combined sources
Beta strandi163 – 1675Combined sources
Turni168 – 1703Combined sources
Beta strandi171 – 1755Combined sources
Beta strandi182 – 1865Combined sources
Helixi194 – 20411Combined sources
Beta strandi208 – 2136Combined sources
Helixi214 – 2163Combined sources
Helixi217 – 22913Combined sources
Beta strandi236 – 2405Combined sources
Beta strandi248 – 2503Combined sources
Helixi253 – 2553Combined sources
Helixi260 – 2667Combined sources
Helixi270 – 2789Combined sources
Beta strandi280 – 2823Combined sources
Helixi293 – 2997Combined sources
Helixi302 – 3043Combined sources
Helixi314 – 32714Combined sources
Helixi330 – 34314Combined sources
Helixi351 – 36111Combined sources
Turni362 – 3643Combined sources
Helixi368 – 3703Combined sources
Helixi371 – 3744Combined sources
Helixi376 – 3783Combined sources
Helixi389 – 3913Combined sources
Helixi392 – 40110Combined sources
Turni402 – 4043Combined sources
Helixi409 – 42315Combined sources
Helixi427 – 43812Combined sources
Beta strandi440 – 4423Combined sources
Helixi447 – 4537Combined sources
Helixi456 – 46611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O5RX-ray2.34A1-469[»]
ProteinModelPortaliQ9X172.
SMRiQ9X172. Positions 1-468.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X172.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi8 – 1811"HIGH" regionAdd
BLAST
Motifi250 – 2545"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
InParanoidiQ9X172.
KOiK09698.
OMAiPEGMLNY.
OrthoDBiEOG6DRPF7.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
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.

Q9X172-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVRVRFAPSP TGFLHVGGAR TALFNFLFAR KEKGKFILRI EDTDLERSER
60 70 80 90 100
EYEEKLMESL RWLGLLWDEG PDVGGDHGPY RQSERVEIYR EHAERLVKEG
110 120 130 140 150
KAYYVYAYPE EIEEMREKLL SEGKAPHYSQ EMFEKFDTPE RRREYEEKGL
160 170 180 190 200
RPAVFFKMPR KDYVLNDVVK GEVVFKTGAI GDFVIMRSNG LPTYNFACVV
210 220 230 240 250
DDMLMEITHV IRGDDHLSNT LRQLALYEAF EKAPPVFAHV STILGPDGKK
260 270 280 290 300
LSKRHGATSV EAFRDMGYLP EALVNYLALL GWSHPEGKEL LTLEELISSF
310 320 330 340 350
SLDRLSPNPA IFDPQKLKWM NGYYLRNMPI EKLAELAKPF FEKAGIKIID
360 370 380 390 400
EEYFKKVLEI TKERVEVLSE FPEESRFFFE DPAPVEIPEE MKEVFSQLKE
410 420 430 440 450
ELQNVRWTME EITPVFKKVL KQHGVKPKEF YMTLRRVLTG REEGPELVNI
460
IPLLGKEIFL RRIERSLGG
Length:469
Mass (Da):54,607
Last modified:November 1, 1999 - v1
Checksum:iF27D3AB4FE070BD8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36422.1.
PIRiG72264.
RefSeqiNP_229152.1. NC_000853.1.
YP_007977707.1. NC_021214.1.
YP_008991558.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD36422; AAD36422; TM_1351.
GeneIDi18093363.
898129.
KEGGitma:TM1351.
PATRICi23937640. VBITheMar51294_1363.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36422.1 .
PIRi G72264.
RefSeqi NP_229152.1. NC_000853.1.
YP_007977707.1. NC_021214.1.
YP_008991558.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2O5R X-ray 2.34 A 1-469 [» ]
ProteinModelPortali Q9X172.
SMRi Q9X172. Positions 1-468.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243274.TM1351.

Proteomic databases

PRIDEi Q9X172.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD36422 ; AAD36422 ; TM_1351 .
GeneIDi 18093363.
898129.
KEGGi tma:TM1351.
PATRICi 23937640. VBITheMar51294_1363.

Phylogenomic databases

eggNOGi COG0008.
InParanoidi Q9X172.
KOi K09698.
OMAi PEGMLNY.
OrthoDBi EOG6DRPF7.

Miscellaneous databases

EvolutionaryTracei Q9X172.

Family and domain databases

Gene3Di 1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPi MF_00022_B. Glu_tRNA_synth_B.
InterProi IPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. "Crystal structure of glutamyl-tRNA synthetase 1 (EC 6.1.1.17) (glutamate-tRNA ligase 1) (glurS 1) (TM1351) from Thermotoga maritima at 2.5 A resolution."
    Joint center for structural genomics (JCSG)
    Submitted (DEC-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS).

Entry informationi

Entry nameiSYE1_THEMA
AccessioniPrimary (citable) accession number: Q9X172
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: November 26, 2014
This is version 104 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3