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Q9HVW9

- HISX_PSEAE

UniProt

Q9HVW9 - HISX_PSEAE

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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 sitei136 – 1361NADUniRule annotation
    Binding sitei197 – 1971NADUniRule annotation
    Binding sitei220 – 2201NADUniRule annotation
    Binding sitei243 – 2431SubstrateUniRule annotation
    Metal bindingi265 – 2651ZincUniRule annotation
    Binding sitei265 – 2651SubstrateUniRule annotation
    Metal bindingi268 – 2681ZincUniRule annotation
    Binding sitei268 – 2681SubstrateUniRule annotation
    Active sitei333 – 3331Proton acceptorUniRule annotation
    Active sitei334 – 3341Proton acceptorUniRule annotation
    Binding sitei334 – 3341SubstrateUniRule annotation
    Metal bindingi367 – 3671ZincUniRule annotation
    Binding sitei367 – 3671SubstrateUniRule annotation
    Binding sitei421 – 4211SubstrateUniRule annotation
    Metal bindingi426 – 4261ZincUniRule annotation
    Binding sitei426 – 4261SubstrateUniRule 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

    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:PA4448
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA4448.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 440440Histidinol dehydrogenasePRO_0000135819Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi208964.PA4448.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HVW9.
    SMRiQ9HVW9. Positions 7-403.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiQKSLHAV.
    OrthoDBiEOG6CVVCR.
    PhylomeDBiQ9HVW9.

    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.

    Q9HVW9-1 [UniParc]FASTAAdd to Basket

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    MTAPFAIRRL NAADPDFGRH LDHLLSWESV SDDSVNQRVL DIIAAVRSRG    50
    DAAVVEFTQR FDGLQAASMA DLILPRERLE LALTRITVAQ REALEVAAER 100
    VRSYHEKQKQ GSWRYTEADG TVLGQQVTPL DRAGLYVPGG KASYPSSVLM 150
    NAIPAKVAGV SEVVMVVPTP RGEINEIVLA AACIAGVDRV FTIGGAQAVA 200
    ALAYGTESVP RVDKIVGPGN IYVATAKRHV FGQVGIDMIA GPSEILVVCD 250
    GQTDPDWIAM DLFSQAEHDE DAQSILVSPD AAFLDRVADS IARLLPTMER 300
    AEIIRTSLEG RGALIQVADQ AQACAVANRI APEHLELSVA DPESWLPEIR 350
    HAGAIFMGRY TAEALGDYCA GPNHVLPTSG TARFSSPLGV YDFQKRSSII 400
    NCSAEGASVL GRTASVLARG ESLTAHARSA EYRILDEKEA 440
    Length:440
    Mass (Da):47,179
    Last modified:March 1, 2001 - v1
    Checksum:i4620B34F7177C98C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004091 Genomic DNA. Translation: AAG07836.1.
    PIRiD83089.
    RefSeqiNP_253138.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG07836; AAG07836; PA4448.
    GeneIDi880992.
    KEGGipae:PA4448.
    PATRICi19843621. VBIPseAer58763_4657.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004091 Genomic DNA. Translation: AAG07836.1 .
    PIRi D83089.
    RefSeqi NP_253138.1. NC_002516.2.

    3D structure databases

    ProteinModelPortali Q9HVW9.
    SMRi Q9HVW9. Positions 7-403.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208964.PA4448.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG07836 ; AAG07836 ; PA4448 .
    GeneIDi 880992.
    KEGGi pae:PA4448.
    PATRICi 19843621. VBIPseAer58763_4657.

    Organism-specific databases

    PseudoCAPi PA4448.

    Phylogenomic databases

    eggNOGi COG0141.
    HOGENOMi HOG000243914.
    KOi K00013.
    OMAi QKSLHAV.
    OrthoDBi EOG6CVVCR.
    PhylomeDBi Q9HVW9.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .

    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: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

    Entry informationi

    Entry nameiHISX_PSEAE
    AccessioniPrimary (citable) accession number: Q9HVW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 89 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