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A5D5L8

- SYE_PELTS

UniProt

A5D5L8 - SYE_PELTS

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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
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 bindingi105 – 1051ZincUniRule annotation
Metal bindingi107 – 1071ZincUniRule annotation
Metal bindingi132 – 1321ZincUniRule annotation
Metal bindingi134 – 1341ZincUniRule annotation
Binding sitei252 – 2521ATPUniRule 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

BioCyciPTHE370438:GCGQ-305-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:PTH_0293
OrganismiPelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
Taxonomic identifieri370438 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaePelotomaculum
ProteomesiUP000006556: 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 – 480480Glutamate--tRNA ligasePRO_0000367732Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi370438.PTH_0293.

Structurei

3D structure databases

ProteinModelPortaliA5D5L8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi8 – 1811"HIGH" regionAdd
BLAST
Motifi249 – 2535"KMSKS" region

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK09698.
OMAiVTGQTHG.
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.

A5D5L8 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVRVRFAPSP TGPLHIGGAR SALFNWLFAR RYGGKFIVRI EDTDLERSSR
60 70 80 90 100
QSEENILAAL RWLGLDWDEG VDAGGPCEPY RQTERLHLYR HYAEILLQSG
110 120 130 140 150
AAYRCYCTEE ELAAEREALM EKGETPRYLG RCRDLTPQER ARLEAEGRKA
160 170 180 190 200
AVRFRVPRDR VIQVKDLVRG DVSFECNGMG DFIIMKSDGI PTYNFAVVVD
210 220 230 240 250
DHTMAISHVI RAEEHLPNTP RQILLYQALG WDTPEFAHVS LILGKDRSKM
260 270 280 290 300
SKRHGATAVE QYREKGYLPE AVVNFLALLG WSPGGENEVL SIEELKQQFS
310 320 330 340 350
LEKVSKSPAV FDLDKLNWLN GYYIRQSSLE RVAELAVPFL EKAGYIRAPL
360 370 380 390 400
SPEEFERVKM MVASVRKYLN CMEEVIDHVK IYFTDNFNNL DEDAREVMAG
410 420 430 440 450
QQVPAVLAAL KDKVASGGKL TGAAARAALK EVGKELGVKG QQIFMPVRVA
460 470 480
VSGNTHGPDL DQIMAILGKD EVVKRLSRWV
Length:480
Mass (Da):54,098
Last modified:June 12, 2007 - v1
Checksum:i89F0E27DD52F19CF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009389 Genomic DNA. Translation: BAF58474.1.
RefSeqiWP_011928373.1. NC_009454.1.
YP_001210843.1. NC_009454.1.

Genome annotation databases

EnsemblBacteriaiBAF58474; BAF58474; PTH_0293.
GeneIDi5139115.
KEGGipth:PTH_0293.
PATRICi22907402. VBIPelThe8413_0328.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009389 Genomic DNA. Translation: BAF58474.1 .
RefSeqi WP_011928373.1. NC_009454.1.
YP_001210843.1. NC_009454.1.

3D structure databases

ProteinModelPortali A5D5L8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 370438.PTH_0293.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAF58474 ; BAF58474 ; PTH_0293 .
GeneIDi 5139115.
KEGGi pth:PTH_0293.
PATRICi 22907402. VBIPelThe8413_0328.

Phylogenomic databases

eggNOGi COG0008.
HOGENOMi HOG000252720.
KOi K09698.
OMAi VTGQTHG.
OrthoDBi EOG6DRPF7.

Enzyme and pathway databases

BioCyci PTHE370438:GCGQ-305-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 genome of Pelotomaculum thermopropionicum reveals niche-associated evolution in anaerobic microbiota."
    Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.
    Genome Res. 18:442-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 13744 / JCM 10971 / SI.

Entry informationi

Entry nameiSYE_PELTS
AccessioniPrimary (citable) accession number: A5D5L8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 12, 2007
Last modified: October 29, 2014
This is version 57 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