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Q65JG7

- Q65JG7_BACLD

UniProt

Q65JG7 - Q65JG7_BACLD

Protein

4-hydroxy-tetrahydrodipicolinate synthase

Gene

dapA1

Organism
Bacillus licheniformis (strain DSM 13 / ATCC 14580)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (25 Oct 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).UniRule annotationSAAS annotation

    Catalytic activityi

    Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H2O.UniRule annotationSAAS annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei45 – 451Part of a proton relay during catalysisUniRule annotation
    Binding sitei46 – 461PyruvateUniRule annotation
    Sitei108 – 1081Part of a proton relay during catalysisUniRule annotation
    Active sitei134 – 1341Proton donor/acceptorUniRule annotation
    Active sitei162 – 1621Schiff-base intermediate with substrateUniRule annotation
    Binding sitei204 – 2041Pyruvate; via carbonyl oxygenUniRule annotation

    GO - Molecular functioni

    1. 4-hydroxy-tetrahydrodipicolinate synthase Source: UniProtKB-EC
    2. amine-lyase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. diaminopimelate biosynthetic process Source: UniProtKB-HAMAP
    2. lysine biosynthetic process via diaminopimelate Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    LyaseUniRule annotationSAAS annotationImported

    Keywords - Biological processi

    Amino-acid biosynthesis, Diaminopimelate biosynthesisUniRule annotationSAAS annotation, Lysine biosynthesisUniRule annotationSAAS annotation

    Keywords - Ligandi

    Schiff baseUniRule annotationSAAS annotation

    Enzyme and pathway databases

    BioCyciBLIC279010:GJ2P-1887-MONOMER.
    MetaCyc:MONOMER-6565.
    UniPathwayiUPA00034; UER00017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-hydroxy-tetrahydrodipicolinate synthaseUniRule annotation (EC:4.3.3.7UniRule annotation)
    Short name:
    HTPA synthaseUniRule annotation
    Gene namesi
    Name:dapA1Imported
    Synonyms:dapAUniRule annotationImported
    Ordered Locus Names:BL01208Imported, BLi01902Imported
    OrganismiBacillus licheniformis (strain DSM 13 / ATCC 14580)Imported
    Taxonomic identifieri279010 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000000608: Chromosome, UP000000606: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotationSAAS annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    CytoplasmUniRule annotationSAAS annotation

    Interactioni

    Subunit structurei

    Homotetramer; dimer of dimers.UniRule annotation

    Protein-protein interaction databases

    STRINGi279010.BL01208.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DapA family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0329.
    HOGENOMiHOG000173604.
    KOiK01714.
    OMAiMLYSGDD.
    OrthoDBiEOG6W7235.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00418. DapA.
    InterProiIPR013785. Aldolase_TIM.
    IPR005263. DapA.
    IPR002220. DapA-like.
    IPR020625. Dihydrodipicolinate_synth_AS.
    IPR020624. Dihydrodipicolinate_synth_CS.
    [Graphical view]
    PANTHERiPTHR12128. PTHR12128. 1 hit.
    PfamiPF00701. DHDPS. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001365. DHDPS. 1 hit.
    PRINTSiPR00146. DHPICSNTHASE.
    TIGRFAMsiTIGR00674. dapA. 1 hit.
    PROSITEiPS00665. DHDPS_1. 1 hit.
    PS00666. DHDPS_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q65JG7-1 [UniParc]FASTAAdd to Basket

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    MNFGNIATAM VTPFDKNENI DFQKLSKLID YLLNNGTDSL VVAGTTGESP    50
    TLSEEEKVAL IQYSVKEAAG RAPIIAGTGS NNTKASIKLT KKAEEAGADA 100
    VMLVTPYYNK PSQEGMYRHF RAIAEETSLP VMLYNVPGRT AASLAPETTI 150
    RLAEIPNIIA IKEASGDLDA ITKIVAETPE DFAVYSGDDS LTLPALSVGA 200
    RGIVSVASHI IGPEMQEMIK HYTEGNTAQA ALIHQKLLPL MKGLFAAPNP 250
    SPLKTALQLK GLDVGSVRLP LIPLNEDERL RLSSLMNGL 289
    Length:289
    Mass (Da):30,917
    Last modified:October 25, 2004 - v1
    Checksum:i56AC182E3E53BEE5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000002 Genomic DNA. Translation: AAU23437.2.
    AE017333 Genomic DNA. Translation: AAU40797.1.
    RefSeqiYP_006713278.1. NC_006322.1.
    YP_079075.2. NC_006270.3.

    Genome annotation databases

    EnsemblBacteriaiAAU23437; AAU23437; BL01208.
    AAU40797; AAU40797; BLi01902.
    GeneIDi3031112.
    3098811.
    KEGGibld:BLi01902.
    bli:BL01208.
    PATRICi18949407. VBIBacLic203714_1907.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000002 Genomic DNA. Translation: AAU23437.2 .
    AE017333 Genomic DNA. Translation: AAU40797.1 .
    RefSeqi YP_006713278.1. NC_006322.1.
    YP_079075.2. NC_006270.3.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 279010.BL01208.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAU23437 ; AAU23437 ; BL01208 .
    AAU40797 ; AAU40797 ; BLi01902 .
    GeneIDi 3031112.
    3098811.
    KEGGi bld:BLi01902.
    bli:BL01208.
    PATRICi 18949407. VBIBacLic203714_1907.

    Phylogenomic databases

    eggNOGi COG0329.
    HOGENOMi HOG000173604.
    KOi K01714.
    OMAi MLYSGDD.
    OrthoDBi EOG6W7235.

    Enzyme and pathway databases

    UniPathwayi UPA00034 ; UER00017 .
    BioCyci BLIC279010:GJ2P-1887-MONOMER.
    MetaCyc:MONOMER-6565.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_00418. DapA.
    InterProi IPR013785. Aldolase_TIM.
    IPR005263. DapA.
    IPR002220. DapA-like.
    IPR020625. Dihydrodipicolinate_synth_AS.
    IPR020624. Dihydrodipicolinate_synth_CS.
    [Graphical view ]
    PANTHERi PTHR12128. PTHR12128. 1 hit.
    Pfami PF00701. DHDPS. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001365. DHDPS. 1 hit.
    PRINTSi PR00146. DHPICSNTHASE.
    TIGRFAMsi TIGR00674. dapA. 1 hit.
    PROSITEi PS00665. DHDPS_1. 1 hit.
    PS00666. DHDPS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 14580Imported and DSM 13 / ATCC 14580 [Goettingen].
    2. "The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
      Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
      J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 13Imported, DSM 13 / ATCC 14580 [Goettingen]Imported and DSM 13 / ATCC 14580 [Novozymes]Imported.
    3. Berka R.M., Rey M.W., Ramaiya P.
      Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: ATCC 14580.
    4. Wiegand S., Hertel R., Dietrich S., Volland S., Liesegang H.
      Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: DSM 13Imported.

    Entry informationi

    Entry nameiQ65JG7_BACLD
    AccessioniPrimary (citable) accession number: Q65JG7
    Secondary accession number(s): Q62UX2
    Entry historyi
    Integrated into UniProtKB/TrEMBL: October 25, 2004
    Last sequence update: October 25, 2004
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Caution

    Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.UniRule annotation

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3