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Q8F393

- HISX_LEPIN

UniProt

Q8F393 - HISX_LEPIN

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.UniRule annotation

    Catalytic activityi

    L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.UniRule annotation

    Cofactori

    Binds 1 zinc ion per subunit.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei125 – 1251NADUniRule annotation
    Binding sitei186 – 1861NADUniRule annotation
    Binding sitei209 – 2091NADUniRule annotation
    Binding sitei234 – 2341SubstrateUniRule annotation
    Metal bindingi256 – 2561ZincUniRule annotation
    Binding sitei256 – 2561SubstrateUniRule annotation
    Metal bindingi259 – 2591ZincUniRule annotation
    Binding sitei259 – 2591SubstrateUniRule annotation
    Active sitei325 – 3251Proton acceptorUniRule annotation
    Active sitei326 – 3261Proton acceptorUniRule annotation
    Binding sitei326 – 3261SubstrateUniRule annotation
    Metal bindingi359 – 3591ZincUniRule annotation
    Binding sitei359 – 3591SubstrateUniRule annotation
    Binding sitei413 – 4131SubstrateUniRule annotation
    Metal bindingi419 – 4191ZincUniRule annotation
    Binding sitei419 – 4191SubstrateUniRule annotation

    GO - Molecular functioni

    1. histidinol dehydrogenase activity Source: UniProtKB-HAMAP
    2. NAD binding Source: InterPro
    3. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. histidine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    BioCyciLINT189518:GJBB-2055-MONOMER.
    UniPathwayiUPA00031; UER00014.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidinol dehydrogenaseUniRule annotation (EC:1.1.1.23UniRule annotation)
    Short name:
    HDHUniRule annotation
    Gene namesi
    Name:hisDUniRule annotation
    Ordered Locus Names:LA_2515
    OrganismiLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
    Taxonomic identifieri189518 [NCBI]
    Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
    ProteomesiUP000001408: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 427427Histidinol dehydrogenasePRO_0000135788Add
    BLAST

    Proteomic databases

    PaxDbiQ8F393.

    Interactioni

    Protein-protein interaction databases

    STRINGi189518.LA2515.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8F393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiYAAKLCG.
    OrthoDBiEOG6CVVCR.

    Family and domain databases

    HAMAPiMF_01024. HisD.
    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR001692. Histidinol_DH_CS.
    IPR022695. Histidinol_DH_monofunct.
    IPR012131. Hstdl_DH.
    [Graphical view]
    PfamiPF00815. Histidinol_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
    PRINTSiPR00083. HOLDHDRGNASE.
    SUPFAMiSSF53720. SSF53720. 1 hit.
    TIGRFAMsiTIGR00069. hisD. 1 hit.
    PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8F393-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAIQIFKVGL KDHSVLDPVL KRAREDLSST LALVKPIVED VKNRGDSALR    50
    EYTQKFDEVI PPKSFVLEIS KLNPKIDPKL KTALVKAAKN IRNFHKIQIP 100
    ENKEIIIHGN KLGILHTPIE SVSVYAPGGK ALYPSTILMG VIPAKLAGVK 150
    NIQIVTPPRK GTLPDGLIAA AKIAGADRIV MAGGAQGIAA VSYGTESIPS 200
    SEFVVGPGNK FVTAAKVYLS GQGVIGIDSP AGPSEVLIIA DDSADPMWVA 250
    ADLLSQAEHG EDSVAILCTN SLSLAQKVKE EVEKALIERP KRGEMKRKSI 300
    KDHGKIFVFS NLEECFVFSN LFAPEHLEIQ TKNFKKDLKK VKHAGSVFLG 350
    NYSPVAMGDY ISGTNHILPT AGAARIYSSL GVSTFLKRVT WQEVSKKSIQ 400
    NLYPHVKVLS EFEGLDEEHG NSVRIRR 427
    Length:427
    Mass (Da):46,380
    Last modified:March 1, 2003 - v1
    Checksum:i2FA9AB963E5D48ED
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE010300 Genomic DNA. Translation: AAN49714.1.
    RefSeqiNP_712696.1. NC_004342.2.

    Genome annotation databases

    EnsemblBacteriaiAAN49714; AAN49714; LA_2515.
    GeneIDi1151858.
    KEGGilil:LA_2515.
    PATRICi22385862. VBILepInt91350_2497.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE010300 Genomic DNA. Translation: AAN49714.1 .
    RefSeqi NP_712696.1. NC_004342.2.

    3D structure databases

    ProteinModelPortali Q8F393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 189518.LA2515.

    Proteomic databases

    PaxDbi Q8F393.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN49714 ; AAN49714 ; LA_2515 .
    GeneIDi 1151858.
    KEGGi lil:LA_2515.
    PATRICi 22385862. VBILepInt91350_2497.

    Phylogenomic databases

    eggNOGi COG0141.
    HOGENOMi HOG000243914.
    KOi K00013.
    OMAi YAAKLCG.
    OrthoDBi EOG6CVVCR.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci LINT189518:GJBB-2055-MONOMER.

    Family and domain databases

    HAMAPi MF_01024. HisD.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR001692. Histidinol_DH_CS.
    IPR022695. Histidinol_DH_monofunct.
    IPR012131. Hstdl_DH.
    [Graphical view ]
    Pfami PF00815. Histidinol_dh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000099. Histidinol_dh. 1 hit.
    PRINTSi PR00083. HOLDHDRGNASE.
    SUPFAMi SSF53720. SSF53720. 1 hit.
    TIGRFAMsi TIGR00069. hisD. 1 hit.
    PROSITEi PS00611. HISOL_DEHYDROGENASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 56601.

    Entry informationi

    Entry nameiHISX_LEPIN
    AccessioniPrimary (citable) accession number: Q8F393
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 88 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3