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Q2RJE3

- SYE_MOOTA

UniProt

Q2RJE3 - SYE_MOOTA

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Moorella thermoacetica (strain ATCC 39073)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (24 Jan 2006)
      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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei254 – 2541ATPUniRule annotation

    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

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMTHE264732:GH0A-1175-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:Moth_1132
    OrganismiMoorella thermoacetica (strain ATCC 39073)
    Taxonomic identifieri264732 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella
    ProteomesiUP000007053: 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 – 490490Glutamate--tRNA ligasePRO_0000237370Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi264732.Moth_1132.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2RJE3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi10 – 2011"HIGH" regionAdd
    BLAST
    Motifi251 – 2555"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252720.
    KOiK01885.
    OMAiDSHEHHA.
    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.

    Q2RJE3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKVRVRFAP SPTGSLHIGG ARTALFNWLF ARHHNGTFVL RIDDTDTERS    50
    TEASYKEILA AMGWLGLDWD EGPEKGGQFG PYLQSQRLEL YRREAARLLN 100
    EGKAYLCYCT VEELAERRRQ AQAEGRPPMY DRRCRYLTPA DRTRLEQEGR 150
    QPVIRLAVPE TGTTVVKDLI RGDVAFENAT IDDFIIFKSN GMPTYNFATV 200
    IDDHLMQISH IIRAEEHLSN TPKQILVYQA LAYELPAFAH VPMILAPDRS 250
    KLSKRHGATS VEEYRDEGYL PEAIINYLAL LGWSPEGEEE IIPLEKIIEQ 300
    FSLERVSKNA AIYDTKKLTW INGHYLREGN LDRITRLALP FLQAKGLLPD 350
    PLPEKDYNYV RSVIAAVRDR VKTLAEVADA ASYFFTDVTN YEEKGIRKHF 400
    TRPGAAALLD EARERLATLP EFNAQAAEEA YRSLAEGKGI STGQLFHPTR 450
    LAISGRTMGP GLFEIMELLG RETVLARLDR AARWIRENLA 490
    Length:490
    Mass (Da):55,581
    Last modified:January 24, 2006 - v1
    Checksum:iA60780CF76C6095D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000232 Genomic DNA. Translation: ABC19446.1.
    RefSeqiYP_429989.1. NC_007644.1.

    Genome annotation databases

    EnsemblBacteriaiABC19446; ABC19446; Moth_1132.
    GeneIDi3833230.
    KEGGimta:Moth_1132.
    PATRICi22639458. VBIMooThe6753_1214.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000232 Genomic DNA. Translation: ABC19446.1 .
    RefSeqi YP_429989.1. NC_007644.1.

    3D structure databases

    ProteinModelPortali Q2RJE3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 264732.Moth_1132.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABC19446 ; ABC19446 ; Moth_1132 .
    GeneIDi 3833230.
    KEGGi mta:Moth_1132.
    PATRICi 22639458. VBIMooThe6753_1214.

    Phylogenomic databases

    eggNOGi COG0008.
    HOGENOMi HOG000252720.
    KOi K01885.
    OMAi DSHEHHA.
    OrthoDBi EOG6DRPF7.

    Enzyme and pathway databases

    BioCyci MTHE264732:GH0A-1175-MONOMER.

    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

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39073.

    Entry informationi

    Entry nameiSYE_MOOTA
    AccessioniPrimary (citable) accession number: Q2RJE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 59 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