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Q4J8I8

- HISX_SULAC

UniProt

Q4J8I8 - HISX_SULAC

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (02 Aug 2005)
      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 sitei112 – 1121NADUniRule annotation
    Binding sitei171 – 1711NADUniRule annotation
    Binding sitei194 – 1941NADUniRule annotation
    Binding sitei217 – 2171SubstrateUniRule annotation
    Metal bindingi239 – 2391ZincUniRule annotation
    Binding sitei239 – 2391SubstrateUniRule annotation
    Metal bindingi242 – 2421ZincUniRule annotation
    Binding sitei242 – 2421SubstrateUniRule annotation
    Active sitei293 – 2931Proton acceptorUniRule annotation
    Active sitei294 – 2941Proton acceptorUniRule annotation
    Binding sitei294 – 2941SubstrateUniRule annotation
    Metal bindingi326 – 3261ZincUniRule annotation
    Binding sitei326 – 3261SubstrateUniRule annotation
    Binding sitei379 – 3791SubstrateUniRule annotation
    Metal bindingi384 – 3841ZincUniRule annotation
    Binding sitei384 – 3841SubstrateUniRule 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

    BioCyciSACI330779:GH9J-1551-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:Saci_1579
    OrganismiSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
    Taxonomic identifieri330779 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    ProteomesiUP000001018: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 393393Histidinol dehydrogenasePRO_0000135905Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi330779.Saci_1579.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4J8I8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiFQEITRE.

    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.

    Q4J8I8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIKYEIPKSR PNEFSKVLPL VEQILNQVKE RGDKALLELE EKYDKAKLDS    50
    LVENRIDELA SKIPEEYKAA IDRIYDQLVE FHKTTLPYMV GGGYNGIEFG 100
    ILWRAIEKVG IYVPGGLKSY PSTLLMAAIP ARVAGVSEIY VATPPNRIDS 150
    VIAYIAKKLK INALYRIGGA QAIAALAYGT ESVKKVDKIV GPGNIFVQAS 200
    KFLVSKDVAI DGIEGPTELV VIADSSADYR HVILDMRAQA EHGSTSYIIL 250
    VTTSDFLIDK VREELDKEEF TYYIVKVKSI DEAIDVANDI APEHLSLFVN 300
    DPKSYLHKIK NAGAISLGKT PPALIDYAAG PDHILPTNAW SRVRGGLTVY 350
    DFLKPISYAN SVNPDKELVN MAKLIAEYEG FIYHSKSIGA RYE 393
    Length:393
    Mass (Da):43,528
    Last modified:August 2, 2005 - v1
    Checksum:i1BD29F2FC3182EB5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000077 Genomic DNA. Translation: AAY80892.1.
    RefSeqiYP_256185.1. NC_007181.1.

    Genome annotation databases

    EnsemblBacteriaiAAY80892; AAY80892; Saci_1579.
    GeneIDi3474262.
    KEGGisai:Saci_1579.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000077 Genomic DNA. Translation: AAY80892.1 .
    RefSeqi YP_256185.1. NC_007181.1.

    3D structure databases

    ProteinModelPortali Q4J8I8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 330779.Saci_1579.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAY80892 ; AAY80892 ; Saci_1579 .
    GeneIDi 3474262.
    KEGGi sai:Saci_1579.

    Phylogenomic databases

    eggNOGi COG0141.
    HOGENOMi HOG000243914.
    KOi K00013.
    OMAi FQEITRE.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci SACI330779:GH9J-1551-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 genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota."
      Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.
      J. Bacteriol. 187:4992-4999(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.

    Entry informationi

    Entry nameiHISX_SULAC
    AccessioniPrimary (citable) accession number: Q4J8I8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2005
    Last sequence update: August 2, 2005
    Last modified: October 1, 2014
    This is version 70 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