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Q65EF9

- HISX_BACLD

UniProt

Q65EF9 - HISX_BACLD

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bacillus licheniformis (strain DSM 13 / ATCC 14580)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (25 Oct 2004)
      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 sitei123 – 1231NADUniRule annotation
    Binding sitei185 – 1851NADUniRule annotation
    Binding sitei208 – 2081NADUniRule annotation
    Binding sitei231 – 2311SubstrateUniRule annotation
    Metal bindingi253 – 2531ZincUniRule annotation
    Binding sitei253 – 2531SubstrateUniRule annotation
    Metal bindingi256 – 2561ZincUniRule annotation
    Binding sitei256 – 2561SubstrateUniRule annotation
    Active sitei321 – 3211Proton acceptorUniRule annotation
    Active sitei322 – 3221Proton acceptorUniRule annotation
    Binding sitei322 – 3221SubstrateUniRule annotation
    Metal bindingi355 – 3551ZincUniRule annotation
    Binding sitei355 – 3551SubstrateUniRule annotation
    Binding sitei409 – 4091SubstrateUniRule annotation
    Metal bindingi414 – 4141ZincUniRule annotation
    Binding sitei414 – 4141SubstrateUniRule 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

    BioCyciBLIC279010:GJ2P-3694-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:BLi03736, BL03408
    OrganismiBacillus licheniformis (strain DSM 13 / ATCC 14580)
    Taxonomic identifieri279010 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000000606: Chromosome, UP000000608: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 426426Histidinol dehydrogenasePRO_0000135727Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi279010.BL03408.

    Structurei

    3D structure databases

    ProteinModelPortaliQ65EF9.
    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.

    Q65EF9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKIKSISGNT SVSLKRSIDA GTEEQRKAVR GIIEEVKKNG NAAVSAFTRQ    50
    FDGADVAGFR VSEEEIKEAY SALEERDLEI IQAAIFNIKE YHERQLATSW 100
    FYHRKDGTML GQKITPLDSA GVYVPGGTAA YPSSVLMNVI PALVAGVDRI 150
    VLASPPGKDG KLSAGVLAAA AELGVTEIYK MGGAQAIAAL AYGTETITPV 200
    DKITGPGNIY VALAKREVFG QVDIDMIAGP SEIAILADST ANYREIAADL 250
    LSQAEHDAMA SSILVTDSET LAESVLKEVY RQLEHLPRKE IARQSIDNYG 300
    LIYVTETMNE AVSVINELAP EHLEILTVQP DALLGQIKHA GAIFLGRYSS 350
    EPVGDYFAGP NHVLPTNGTA RFSSPLNVTD FQKRSSIISY SREAFRANAE 400
    KIAAFARLEG LEAHARAIES RNREED 426
    Length:426
    Mass (Da):46,028
    Last modified:October 25, 2004 - v1
    Checksum:i76A087539E215CA8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017333 Genomic DNA. Translation: AAU42555.1.
    CP000002 Genomic DNA. Translation: AAU25184.1.
    RefSeqiYP_006715017.1. NC_006322.1.
    YP_080822.1. NC_006270.3.

    Genome annotation databases

    EnsemblBacteriaiAAU25184; AAU25184; BL03408.
    AAU42555; AAU42555; BLi03736.
    GeneIDi3027872.
    3100933.
    KEGGibld:BLi03736.
    bli:BL03408.
    PATRICi18953260. VBIBacLic203714_3805.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017333 Genomic DNA. Translation: AAU42555.1 .
    CP000002 Genomic DNA. Translation: AAU25184.1 .
    RefSeqi YP_006715017.1. NC_006322.1.
    YP_080822.1. NC_006270.3.

    3D structure databases

    ProteinModelPortali Q65EF9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 279010.BL03408.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAU25184 ; AAU25184 ; BL03408 .
    AAU42555 ; AAU42555 ; BLi03736 .
    GeneIDi 3027872.
    3100933.
    KEGGi bld:BLi03736.
    bli:BL03408.
    PATRICi 18953260. VBIBacLic203714_3805.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci BLIC279010:GJ2P-3694-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. "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 13 / ATCC 14580.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 13 / ATCC 14580.

    Entry informationi

    Entry nameiHISX_BACLD
    AccessioniPrimary (citable) accession number: Q65EF9
    Secondary accession number(s): Q62PX7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: October 25, 2004
    Last modified: October 1, 2014
    This is version 78 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