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P45631

- SYE_AZOBR

UniProt

P45631 - SYE_AZOBR

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Azospirillum brasilense
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 2 (15 Dec 1998)
      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 sitei243 – 2431ATPUniRule 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

    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
    OrganismiAzospirillum brasilense
    Taxonomic identifieri192 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

    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 – 446446Glutamate--tRNA ligasePRO_0000119496Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliP45631.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi9 – 1911"HIGH" regionAdd
    BLAST
    Motifi240 – 2445"KMSKS" region

    Sequence similaritiesi

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

    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.

    P45631-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVAVPFAPS PTGLLHVGNV RLALVNWLFA RKAGGNFLVR LDDTDEERSK    50
    PEYAEGIERD LTWLGLTWDR FARESDRYGA TDEVAAALKA SGRLYPCYET 100
    PEELNLKRAS LSSQGRPPIY DRAALRLGDA DRARLEAEGR KPHWRFKLEH 150
    TPVEWTDLVR GPVHFEGSAL SDPVLIAEDG RPLYTLTSVV DDADLAITHV 200
    IRGEDHLANT AVQIQIFEAV GGAVPVFAHL PLLTDATGQG LSKRLGSLSV 250
    ASLREEEGIE PMALASLLAK LGTSDAIEPR LTLDELVAEF DIAKVSRATP 300
    KFDPEELLRL NARILHLLPF ERVAGELAAS VWMMPTPAFW EAVPNLSRVA 350
    EARDWWAVTH APVARRRTIP LFLAEAATLL PKEPWDLSTW GTWTGAVKAK 400
    TGRKGKDLFL PLRRALTGRD HGGQLKNLLP LIGRTRAHKR LAGETA 446
    Length:446
    Mass (Da):49,179
    Last modified:December 15, 1998 - v2
    Checksum:iA7CE141B79416572
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61P → R in AAA61907. 1 PublicationCurated
    Sequence conflicti39 – 391V → L in AAA61907. 1 PublicationCurated
    Sequence conflicti80 – 812AT → RY in AAA61907. 1 PublicationCurated
    Sequence conflicti112 – 1121S → V in AAA61907. 1 PublicationCurated
    Sequence conflicti137 – 1371A → S in AAA61907. 1 PublicationCurated
    Sequence conflicti142 – 1421P → R in AAA61907. 1 PublicationCurated
    Sequence conflicti168 – 1681S → A in AAA61907. 1 PublicationCurated
    Sequence conflicti177 – 1771A → R in AAA61907. 1 PublicationCurated
    Sequence conflicti207 – 2071L → V in AAA61907. 1 PublicationCurated
    Sequence conflicti220 – 2234VGGA → LTNSEGGGV1 PublicationCurated
    Sequence conflicti378 – 3781T → A in AAA61907. 1 PublicationCurated
    Sequence conflicti382 – 3821K → E in AAA61907. 1 PublicationCurated
    Sequence conflicti423 – 4242GQ → PE in AAA61907. 1 PublicationCurated
    Sequence conflicti438 – 4381H → E in AAA61907. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17699 Genomic DNA. Translation: AAA61907.1.
    X99587 Genomic DNA. Translation: CAA67900.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17699 Genomic DNA. Translation: AAA61907.1 .
    X99587 Genomic DNA. Translation: CAA67900.1 .

    3D structure databases

    ProteinModelPortali P45631.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. Costacurta A., Keijers V., Vanderleyden J.
      Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Sp245.
    2. "Identification and isolation of the indole-3-pyruvate decarboxylase gene from Azospirillum brasilense Sp7: sequencing and functional analysis of the gene locus."
      Zimmer W., Wesche M., Timmermans L.
      Curr. Microbiol. 36:327-331(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 29145 / Sp7 / DSM 1690 / IMET 11303.

    Entry informationi

    Entry nameiSYE_AZOBR
    AccessioniPrimary (citable) accession number: P45631
    Secondary accession number(s): O07044
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 82 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3