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A5D5L8

- SYE_PELTS

UniProt

A5D5L8 - SYE_PELTS

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
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (12 Jun 2007)
      Previous versions | rss
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    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

    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-SubCell

    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.

    A5D5L8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVRVRFAPSP TGPLHIGGAR SALFNWLFAR RYGGKFIVRI EDTDLERSSR    50
    QSEENILAAL RWLGLDWDEG VDAGGPCEPY RQTERLHLYR HYAEILLQSG 100
    AAYRCYCTEE ELAAEREALM EKGETPRYLG RCRDLTPQER ARLEAEGRKA 150
    AVRFRVPRDR VIQVKDLVRG DVSFECNGMG DFIIMKSDGI PTYNFAVVVD 200
    DHTMAISHVI RAEEHLPNTP RQILLYQALG WDTPEFAHVS LILGKDRSKM 250
    SKRHGATAVE QYREKGYLPE AVVNFLALLG WSPGGENEVL SIEELKQQFS 300
    LEKVSKSPAV FDLDKLNWLN GYYIRQSSLE RVAELAVPFL EKAGYIRAPL 350
    SPEEFERVKM MVASVRKYLN CMEEVIDHVK IYFTDNFNNL DEDAREVMAG 400
    QQVPAVLAAL KDKVASGGKL TGAAARAALK EVGKELGVKG QQIFMPVRVA 450
    VSGNTHGPDL DQIMAILGKD EVVKRLSRWV 480
    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 1, 2014
    This is version 56 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