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Q976J8

- LYSW_SULTO

UniProt

Q976J8 - LYSW_SULTO

Protein

Alpha-aminoadipate/glutamate carrier protein LysW

Gene

lysW

Organism
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Carrier protein that bears the covalently bound substrates for arginine and lysine biosynthesis; bound L-glutamate is sequentially converted to L-ornithine, while bound alpha-aminoadipate (AAA) is sequentially converted to L-lysine.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi6 – 61Zinc
    Metal bindingi9 – 91Zinc
    Metal bindingi27 – 271Zinc
    Metal bindingi29 – 291Zinc

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1 – 3434TFIIB-typeAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. arginine biosynthetic process Source: UniProtKB-UniPathway
    2. lysine biosynthetic process via aminoadipic acid Source: UniProtKB-UniPathway

    Keywords - Biological processi

    Amino-acid biosynthesis, Arginine biosynthesis, Lysine biosynthesis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciSTOK273063:GJC7-212-MONOMER.
    UniPathwayiUPA00033.
    UPA00068.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-aminoadipate/glutamate carrier protein LysW
    Alternative name(s):
    AAA carrier protein LysW
    Gene namesi
    Name:lysW
    Ordered Locus Names:STK_01925
    ORF Names:STS023
    OrganismiSulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
    Taxonomic identifieri273063 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    ProteomesiUP000001015: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5656Alpha-aminoadipate/glutamate carrier protein LysWPRO_0000084538Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei56 – 5615-glutamyl 2-aminoadipic acid; alternate
    Modified residuei56 – 5615-glutamyl glutamate; alternate
    Modified residuei56 – 5615-glutamyl N2-lysine; alternateCurated
    Modified residuei56 – 5615-glutamyl N2-ornithine; alternateCurated

    Post-translational modificationi

    Formation of an isopeptide bond between the gamma-carboxyl group of the C-terminal glutamate and the amino group of alpha-aminoadipate (AAA) is catalyzed by LysX. The bound AAA is then converted to L-lysine in a series of reactions catalyzed by LysZ, LysY and LysJ. Release of the product L-lysine is catalyzed by LysK. Formation of an isopeptide bond between the gamma-carboxyl group of the C-terminal glutamate and the amino group of L-glutamate is catalyzed by ArgX. The bound substrate is then sequentially converted to ornithine which is eventually converted to L-arginine (PubMed:23434852).1 Publication

    Keywords - PTMi

    Isopeptide bond

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi273063.STS023.

    Structurei

    Secondary structure

    1
    56
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 54
    Turni7 – 93
    Beta strandi12 – 154
    Beta strandi24 – 263
    Beta strandi32 – 387
    Beta strandi41 – 466

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VPBX-ray1.80E/F1-56[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi50 – 501EDWGE

    Sequence similaritiesi

    Contains 1 TFIIB-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1 – 3434TFIIB-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG252918.
    HOGENOMiHOG000105320.
    KOiK05826.
    OMAiEIVEHEC.

    Sequencei

    Sequence statusi: Complete.

    Q976J8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVVLKCPVCN GDVNVPDDAL PGEIVEHECG AQLEVYNDHG RLALRLAEQV   50
    GEDWGE 56
    Length:56
    Mass (Da):6,104
    Last modified:December 1, 2001 - v1
    Checksum:iC72792074AD8585A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000023 Genomic DNA. Translation: BAB65149.1.
    RefSeqiNP_376040.1. NC_003106.2.

    Genome annotation databases

    EnsemblBacteriaiBAB65149; BAB65149; STK_01925.
    GeneIDi1458077.
    KEGGisto:STS023.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000023 Genomic DNA. Translation: BAB65149.1 .
    RefSeqi NP_376040.1. NC_003106.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VPB X-ray 1.80 E/F 1-56 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273063.STS023.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB65149 ; BAB65149 ; STK_01925 .
    GeneIDi 1458077.
    KEGGi sto:STS023.

    Phylogenomic databases

    eggNOGi NOG252918.
    HOGENOMi HOG000105320.
    KOi K05826.
    OMAi EIVEHEC.

    Enzyme and pathway databases

    UniPathwayi UPA00033 .
    UPA00068 .
    BioCyci STOK273063:GJC7-212-MONOMER.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 16993 / JCM 10545 / NBRC 100140 / 7.
    2. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ZINC AND ARGX, FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiLYSW_SULTO
    AccessioniPrimary (citable) accession number: Q976J8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: December 1, 2001
    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

    Miscellaneous

    Binds zinc ions via its zinc finger domain, as shown by X-ray crystallography (PubMed:23434852). In contrast, the absorption spectrum of the ortholog from Thermophilus suggests that it may bind iron ions, possibly via the predicted zinc finger domain.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3