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Q8ZY17

- HISX_PYRAE

UniProt

Q8ZY17 - HISX_PYRAE

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      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 sitei197 – 1971SubstrateUniRule annotation
    Metal bindingi218 – 2181ZincUniRule annotation
    Binding sitei218 – 2181SubstrateUniRule annotation
    Metal bindingi221 – 2211ZincUniRule annotation
    Binding sitei221 – 2211SubstrateUniRule annotation
    Active sitei276 – 2761Proton acceptorUniRule annotation
    Active sitei277 – 2771Proton acceptorUniRule annotation
    Binding sitei277 – 2771SubstrateUniRule annotation
    Metal bindingi306 – 3061ZincUniRule annotation
    Binding sitei306 – 3061SubstrateUniRule annotation
    Binding sitei358 – 3581SubstrateUniRule annotation
    Metal bindingi363 – 3631ZincUniRule annotation
    Binding sitei363 – 3631SubstrateUniRule 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

    BioCyciPAER178306:GCEO-707-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:PAE0988
    OrganismiPyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
    Taxonomic identifieri178306 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
    ProteomesiUP000002439: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 368368Histidinol dehydrogenasePRO_0000135902Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi178306.PAE0988.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8ZY17.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiNAMSILL.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q8ZY17-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRGFPREVLE SVWKIVDDVQ SGGLKAALEY SKRLDGVAPE PHLVTPRQGG    50
    DPEVVSAALA AAKSLEALYS RISPPAAVDF YGGILRQILW KPVRRAALYV 100
    PARYISTLVM LAVPARLAGV EEVYVVTPPR GVSEELLAVA KELGVKAVLA 150
    LGGPHGLAYA VFHMGVDVVA GPGGLYVQAA KYILSQYVGI DGIEGPTELV 200
    IYAEGVPPEV AVRGALAQLE HGPTSFAYLL SPDGELLKKA EELYVRERTS 250
    SMGPLKVKKV GGIDEAVSFI DEIAPEHLEV WGRREVAYRV RNVGAVSVNM 300
    PSPYLDYVAG ISHVLPTGGT ARWRGVITPL AFMKPIGIAE AVGELTLREA 350
    ARKLAEYEGF KYHGEALR 368
    Length:368
    Mass (Da):39,541
    Last modified:March 1, 2002 - v1
    Checksum:i7346BE8A2B0333EA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009441 Genomic DNA. Translation: AAL63179.1.
    RefSeqiNP_558997.1. NC_003364.1.
    WP_011007651.1. NC_003364.1.

    Genome annotation databases

    EnsemblBacteriaiAAL63179; AAL63179; PAE0988.
    GeneIDi1465414.
    KEGGipai:PAE0988.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009441 Genomic DNA. Translation: AAL63179.1 .
    RefSeqi NP_558997.1. NC_003364.1.
    WP_011007651.1. NC_003364.1.

    3D structure databases

    ProteinModelPortali Q8ZY17.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 178306.PAE0988.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL63179 ; AAL63179 ; PAE0988 .
    GeneIDi 1465414.
    KEGGi pai:PAE0988.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci PAER178306:GCEO-707-MONOMER.

    Family and domain databases

    HAMAPi MF_01024. HisD.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR001692. Histidinol_DH_CS.
    IPR012131. Hstdl_DH.
    [Graphical view ]
    Pfami PF00815. Histidinol_dh. 1 hit.
    [Graphical view ]
    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. "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum."
      Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., Miller J.H.
      Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827.

    Entry informationi

    Entry nameiHISX_PYRAE
    AccessioniPrimary (citable) accession number: Q8ZY17
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 85 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