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A8G3I8

- SYE_PROM2

UniProt

A8G3I8 - SYE_PROM2

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Prochlorococcus marinus (strain MIT 9215)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (13 Nov 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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei251 – 2511ATPUniRule 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

    BioCyciPMAR93060:GI08-574-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:P9215_05531
    OrganismiProchlorococcus marinus (strain MIT 9215)
    Taxonomic identifieri93060 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
    ProteomesiUP000002014: 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 – 479479Glutamate--tRNA ligasePRO_1000057198Add
    BLAST

    Proteomic databases

    PRIDEiA8G3I8.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi93060.P9215_05531.

    Structurei

    3D structure databases

    ProteinModelPortaliA8G3I8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi9 – 1911"HIGH" regionAdd
    BLAST
    Motifi248 – 2525"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252720.
    KOiK01885.
    OMAiDIDMQIS.
    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.

    A8G3I8-1 [UniParc]FASTAAdd to Basket

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    MEKRLRLAPS PTGLFHIGTA RTALFNWLYA QKIGGKFLLR IEDTDFVRSK    50
    SEYTKNILEG LKWLGLKWDD EILKQSDRIS IHKSYIKKLL ECGAAYRCFT 100
    TENEISELRE EQKNKGLPPK HDNRHRSLSK EEIDSFISQG KTSVIRFKID 150
    EKIEIKWVDL IRGEIKWQGK DLGGDLVLSR RAKGYEIGDP LYNLAVVVDD 200
    NFMNITHVVR GEDHISNTAK QILIYEALNF KLPTFSHTPL ILNNEGKKLS 250
    KRDCVTSIDE FRDMGYLPEA LSNYMAFLGW SPKSTDREIL SLNEISEIFD 300
    LSDINKAGAK FSWEKLNWIN SQYIKNMESI KLSEIIRKYW DDNGWVAPSQ 350
    EWAHKLAILI RDSMILLKDA IDQSKPFFLI PKIKKEGQDF LENNDSKASL 400
    RLILNYLIEQ NAIKLNKEKA KEIINEISKM HNVKKGILMK SLRVAFFGSL 450
    SGPDLIQSWE LFSESKTDIS RIERCFKSI 479
    Length:479
    Mass (Da):55,430
    Last modified:November 13, 2007 - v1
    Checksum:iD69389C1F08CFB8C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000825 Genomic DNA. Translation: ABV50169.1.
    RefSeqiYP_001483755.1. NC_009840.1.

    Genome annotation databases

    EnsemblBacteriaiABV50169; ABV50169; P9215_05531.
    GeneIDi5615840.
    KEGGipmh:P9215_05531.
    PATRICi22990560. VBIProMar119824_0558.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000825 Genomic DNA. Translation: ABV50169.1 .
    RefSeqi YP_001483755.1. NC_009840.1.

    3D structure databases

    ProteinModelPortali A8G3I8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 93060.P9215_05531.

    Proteomic databases

    PRIDEi A8G3I8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABV50169 ; ABV50169 ; P9215_05531 .
    GeneIDi 5615840.
    KEGGi pmh:P9215_05531.
    PATRICi 22990560. VBIProMar119824_0558.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PMAR93060:GI08-574-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MIT 9215.

    Entry informationi

    Entry nameiSYE_PROM2
    AccessioniPrimary (citable) accession number: A8G3I8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 48 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

    Documents

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

    External Data

    Dasty 3