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B0KQJ5

- B0KQJ5_PSEPG

UniProt

B0KQJ5 - B0KQJ5_PSEPG

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Pseudomonas putida (strain GB-1)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (18 Mar 2008)
      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 annotationSAAS annotation

    Catalytic activityi

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

    Cofactori

    Binds 1 zinc ion per subunit.UniRule annotationSAAS 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

    OxidoreductaseUniRule annotationSAAS annotationImported

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesisUniRule annotationSAAS annotation

    Keywords - Ligandi

    Metal-bindingUniRule annotationSAAS annotation, NADUniRule annotationSAAS annotation, ZincUniRule annotationSAAS annotation

    Enzyme and pathway databases

    BioCyciPPUT76869:GIXB-1004-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:PputGB1_0973Imported
    OrganismiPseudomonas putida (strain GB-1)Imported
    Taxonomic identifieri76869 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002157: Chromosome

    Interactioni

    Protein-protein interaction databases

    STRINGi76869.PputGB1_0973.

    Structurei

    3D structure databases

    ProteinModelPortaliB0KQJ5.
    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.

    B0KQJ5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTVSTAIARL NAADPDFARH LDHLLSWESV SDDAVNQRVL DIIKAVRERG    50
    DAALVEFTQR FDGVDAKSIE DLILNRERLE LALTRITPIQ REALEKAANR 100
    VRMYHERQKQ DSWQYTEADG TVLGQKVTPL DRAGLYVPGG KASYPSSVLM 150
    NAIPAKVAGV AEVVMVVPTP RGEVNELVLA AACIAGVDRV FTVGGAQAVA 200
    ALAYGTESVP QVDKIVGPGN IYVATAKRHV FGQVGIDMIA GPSEILVVCD 250
    GQTDPDWIAM DLFSQAEHDE DAQAILVSPD AAFLDRVAAS IDKLMPTMER 300
    AEIIEKSING RGALIQVRDM QQAMDVANRI APEHLELSVA DPQAWLPHIR 350
    HAGAIFMGRH TSEALGDYCA GPNHVLPTSG TARFSSPLGV YDFQKRSSII 400
    FCSEQGASEL GHTASVLARG ESLTAHARSA EYRILTQDKG N 441
    Length:441
    Mass (Da):47,678
    Last modified:March 18, 2008 - v1
    Checksum:iA2FA13FFCBF97561
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000926 Genomic DNA. Translation: ABY96883.1.
    RefSeqiWP_012270669.1. NC_010322.1.
    YP_001667219.1. NC_010322.1.

    Genome annotation databases

    EnsemblBacteriaiABY96883; ABY96883; PputGB1_0973.
    GeneIDi5868733.
    KEGGippg:PputGB1_0973.
    PATRICi19928921. VBIPsePut76638_0980.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000926 Genomic DNA. Translation: ABY96883.1 .
    RefSeqi WP_012270669.1. NC_010322.1.
    YP_001667219.1. NC_010322.1.

    3D structure databases

    ProteinModelPortali B0KQJ5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 76869.PputGB1_0973.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABY96883 ; ABY96883 ; PputGB1_0973 .
    GeneIDi 5868733.
    KEGGi ppg:PputGB1_0973.
    PATRICi 19928921. VBIPsePut76638_0980.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci PPUT76869:GIXB-1004-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: GB-1Imported.

    Entry informationi

    Entry nameiB0KQJ5_PSEPG
    AccessioniPrimary (citable) accession number: B0KQJ5
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 18, 2008
    Last sequence update: March 18, 2008
    Last modified: October 1, 2014
    This is version 53 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteomeImported

    External Data

    Dasty 3