Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A1UEA6

- SYE_MYCSK

UniProt

A1UEA6 - SYE_MYCSK

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Mycobacterium sp. (strain KMS)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (06 Feb 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei259 – 2591ATPUniRule 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

    BioCyciMSP189918:GH4X-1976-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:Mkms_1965
    OrganismiMycobacterium sp. (strain KMS)
    Taxonomic identifieri189918 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000638: 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_0000330982Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi189918.Mkms_1965.

    Structurei

    3D structure databases

    ProteinModelPortaliA1UEA6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi12 – 2211"HIGH" regionAdd
    BLAST
    Motifi256 – 2605"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252722.
    KOiK01885.
    OMAiPEGMLNY.
    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.
    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.

    Sequencei

    Sequence statusi: Complete.

    A1UEA6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNDMAVRVRF CPSPTGTPHV GLIRTALFNW AYARHTGGTF VFRIEDTDSA    50
    RDSEESYQAI LDALNWLGLD YDEGPEIGGP YAPYRQSQRR DLYRDVIDRL 100
    IAAGEAYEAY STAEEVEARH LAAGRNPKLG YDNFDRDLTD EQRAAHRAEG 150
    RNPVIRLRMP ERDITWRDLV RGETTFGAGT MPDFALTRGN GEPLYTLVNP 200
    VDDALMKITH VLRGEDLLPS TPRQIALYEA LIRIGVADGV PEFAHLPSVL 250
    GDGNKKLSKR DPQSNLFLHR DRGFIPEGLL NYLALLGWGI ADDRDVFSLD 300
    EMVAAFDVVD VNSNPARFDQ KKADALNAEH IRLLSEDEFT ARLKAYFAAH 350
    GHDTGLDDAQ FAEAARLVQT RIVVLGDAWG LLKFLDEGAF VLDEKAAAKE 400
    LKADAVPVLD AALAGLEGVG QWTTGAIEEA LKKALLEDLE LKPRKAFGPI 450
    RVAATGASVS PPLFESLELL GRDRSLARLR AGRDHAAAAA 490
    Length:490
    Mass (Da):53,983
    Last modified:February 6, 2007 - v1
    Checksum:i4AE5F763E87FBE1D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000518 Genomic DNA. Translation: ABL91164.1.
    RefSeqiYP_937954.1. NC_008705.1.

    Genome annotation databases

    EnsemblBacteriaiABL91164; ABL91164; Mkms_1965.
    GeneIDi4613711.
    KEGGimkm:Mkms_1965.
    PATRICi18102842. VBIMycSp70743_2465.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000518 Genomic DNA. Translation: ABL91164.1 .
    RefSeqi YP_937954.1. NC_008705.1.

    3D structure databases

    ProteinModelPortali A1UEA6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 189918.Mkms_1965.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABL91164 ; ABL91164 ; Mkms_1965 .
    GeneIDi 4613711.
    KEGGi mkm:Mkms_1965.
    PATRICi 18102842. VBIMycSp70743_2465.

    Phylogenomic databases

    eggNOGi COG0008.
    HOGENOMi HOG000252722.
    KOi K01885.
    OMAi PEGMLNY.
    OrthoDBi EOG6DRPF7.

    Enzyme and pathway databases

    BioCyci MSP189918:GH4X-1976-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.
    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.
    ProtoNeti Search...

    Publicationsi

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

    Entry informationi

    Entry nameiSYE_MYCSK
    AccessioniPrimary (citable) accession number: A1UEA6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 60 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