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)

Q5SH23

- LYSX_THET8

UniProt

Q5SH23 - LYSX_THET8

Protein

Alpha-aminoadipate--LysW ligase LysX

Gene

lysX

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the ATP-dependent formation of a covalent bond between the amino group of alpha-aminoadipate (AAA) and the gamma-carboxyl group of the C-terminal glutamate residue in LysW.1 Publication

    Catalytic activityi

    ATP + [LysW] + L-2-aminoadipate = ADP + phosphate + [LysW]-L-2-aminoadipate.1 Publication

    Cofactori

    Binds 2 magnesium ions per subunit.By similarity

    Kineticsi

    1. KM=2.1 mM for alpha-aminoadipate1 Publication
    2. KM=2.6 mM for ATP1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei89 – 891ATPBy similarity
    Binding sitei129 – 1291ATP
    Binding sitei194 – 1941ATP
    Binding sitei202 – 2021ATPBy similarity
    Metal bindingi237 – 2371Magnesium 1By similarity
    Metal bindingi249 – 2491Magnesium 1By similarity
    Metal bindingi249 – 2491Magnesium 2By similarity
    Metal bindingi251 – 2511Magnesium 2By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi133 – 1397ATP
    Nucleotide bindingi169 – 18012ATPAdd
    BLAST

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: UniProtKB-EC
    2. ATP binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cellular protein modification process Source: InterPro
    2. lysine biosynthetic process via aminoadipic acid Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Amino-acid biosynthesis, Lysine biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-6728.
    TTHE300852:GH8R-1953-MONOMER.
    UniPathwayiUPA00033; UER00035.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-aminoadipate--LysW ligase LysX (EC:6.3.2.n4)
    Short name:
    AAA--LysW ligase LysX
    Gene namesi
    Name:lysX
    Ordered Locus Names:TTHA1907
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000532: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 280280Alpha-aminoadipate--LysW ligase LysXPRO_0000391001Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    STRINGi300852.TTHA1907.

    Structurei

    Secondary structure

    1
    280
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 87
    Helixi11 – 2212
    Beta strandi27 – 315
    Helixi32 – 343
    Helixi44 – 463
    Beta strandi51 – 544
    Helixi59 – 7113
    Beta strandi76 – 783
    Helixi80 – 878
    Helixi89 – 9911
    Beta strandi106 – 1116
    Helixi112 – 12211
    Beta strandi124 – 1296
    Beta strandi140 – 1423
    Helixi145 – 15814
    Helixi161 – 1644
    Beta strandi165 – 1706
    Beta strandi175 – 18410
    Beta strandi187 – 1959
    Beta strandi197 – 2004
    Helixi203 – 2053
    Beta strandi208 – 2114
    Helixi216 – 22813
    Beta strandi232 – 24110
    Beta strandi244 – 25310
    Helixi259 – 2635
    Helixi267 – 27711

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UC8X-ray2.00A/B1-280[»]
    1UC9X-ray2.38A/B1-280[»]
    3VPDX-ray1.95A/B1-279[»]
    ProteinModelPortaliQ5SH23.
    SMRiQ5SH23. Positions 1-280.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5SH23.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini93 – 276184ATP-graspPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi258 – 2592N-[TS] motif that is essential for LysX substrate specificity

    Sequence similaritiesi

    Belongs to the RimK family. LysX subfamily.Curated
    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0189.
    HOGENOMiHOG000228553.
    KOiK05827.
    OMAiACMERIA.
    OrthoDBiEOG6DZDX8.
    PhylomeDBiQ5SH23.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    InterProiIPR011761. ATP-grasp.
    IPR013651. ATP-grasp_RimK-type.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR011870. LysX_arch.
    IPR016185. PreATP-grasp_dom.
    IPR004666. RpS6_RimK/Lys_biosynth_LsyX.
    [Graphical view]
    PfamiPF08443. RimK. 1 hit.
    [Graphical view]
    SUPFAMiSSF52440. SSF52440. 1 hit.
    TIGRFAMsiTIGR02144. LysX_arch. 1 hit.
    TIGR00768. rimK_fam. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5SH23-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLAILYDRIR PDERMLFERA EALGLPYKKV YVPALPMVLG ERPKELEGVT    50
    VALERCVSQS RGLAAARYLT ALGIPVVNRP EVIEACGDKW ATSVALAKAG 100
    LPQPKTALAT DREEALRLME AFGYPVVLKP VIGSWGRLLA KVTDRAAAEA 150
    LLEHKEVLGG FQHQLFYIQE YVEKPGRDIR VFVVGERAIA AIYRRSAHWI 200
    TNTARGGQAE NCPLTEEVAR LSVKAAEAVG GGVVAVDLFE SERGLLVNEV 250
    NHTMEFKNSV HTTGVDIPGE ILKYAWSLAS 280
    Length:280
    Mass (Da):30,718
    Last modified:December 21, 2004 - v1
    Checksum:iB168629146AF1344
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB103032 Genomic DNA. Translation: BAC67243.1.
    AP008226 Genomic DNA. Translation: BAD71730.1.
    RefSeqiWP_011229004.1. NC_006461.1.
    YP_145173.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD71730; BAD71730; BAD71730.
    GeneIDi3167971.
    KEGGittj:TTHA1907.
    PATRICi23958779. VBITheThe93045_1875.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB103032 Genomic DNA. Translation: BAC67243.1 .
    AP008226 Genomic DNA. Translation: BAD71730.1 .
    RefSeqi WP_011229004.1. NC_006461.1.
    YP_145173.1. NC_006461.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UC8 X-ray 2.00 A/B 1-280 [» ]
    1UC9 X-ray 2.38 A/B 1-280 [» ]
    3VPD X-ray 1.95 A/B 1-279 [» ]
    ProteinModelPortali Q5SH23.
    SMRi Q5SH23. Positions 1-280.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 300852.TTHA1907.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD71730 ; BAD71730 ; BAD71730 .
    GeneIDi 3167971.
    KEGGi ttj:TTHA1907.
    PATRICi 23958779. VBITheThe93045_1875.

    Phylogenomic databases

    eggNOGi COG0189.
    HOGENOMi HOG000228553.
    KOi K05827.
    OMAi ACMERIA.
    OrthoDBi EOG6DZDX8.
    PhylomeDBi Q5SH23.

    Enzyme and pathway databases

    UniPathwayi UPA00033 ; UER00035 .
    BioCyci MetaCyc:MONOMER-6728.
    TTHE300852:GH8R-1953-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q5SH23.

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    InterProi IPR011761. ATP-grasp.
    IPR013651. ATP-grasp_RimK-type.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR011870. LysX_arch.
    IPR016185. PreATP-grasp_dom.
    IPR004666. RpS6_RimK/Lys_biosynth_LsyX.
    [Graphical view ]
    Pfami PF08443. RimK. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52440. SSF52440. 1 hit.
    TIGRFAMsi TIGR02144. LysX_arch. 1 hit.
    TIGR00768. rimK_fam. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Crystal structure of a lysine biosynthesis enzyme, LysX, from Thermus thermophilus HB8."
      Sakai H., Vassylyeva M.N., Matsuura T., Sekine S., Gotoh K., Nishiyama M., Terada T., Shirouzu M., Kuramitsu S., Vassylyev D.G., Yokoyama S.
      J. Mol. Biol. 332:729-740(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP, SUBUNIT.
      Strain: HB8 / ATCC 27634 / DSM 579.
    2. "Complete genome sequence of Thermus thermophilus HB8."
      Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HB8 / ATCC 27634 / DSM 579.
    3. "Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus."
      Horie A., Tomita T., Saiki A., Kono H., Taka H., Mineki R., Fujimura T., Nishiyama C., Kuzuyama T., Nishiyama M.
      Nat. Chem. Biol. 5:673-679(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    4. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ATP ANALOG.

    Entry informationi

    Entry nameiLYSX_THET8
    AccessioniPrimary (citable) accession number: Q5SH23
    Secondary accession number(s): Q84BR0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 19, 2010
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 71 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

    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