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P59397

- HISX_BRADU

UniProt

P59397 - HISX_BRADU

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (25 Mar 2003)
      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 sitei130 – 1301NADUniRule annotation
    Binding sitei191 – 1911NADUniRule annotation
    Binding sitei214 – 2141NADUniRule annotation
    Binding sitei237 – 2371SubstrateUniRule annotation
    Metal bindingi259 – 2591ZincUniRule annotation
    Binding sitei259 – 2591SubstrateUniRule annotation
    Metal bindingi262 – 2621ZincUniRule annotation
    Binding sitei262 – 2621SubstrateUniRule annotation
    Active sitei327 – 3271Proton acceptorUniRule annotation
    Active sitei328 – 3281Proton acceptorUniRule annotation
    Binding sitei328 – 3281SubstrateUniRule annotation
    Metal bindingi361 – 3611ZincUniRule annotation
    Binding sitei361 – 3611SubstrateUniRule annotation
    Binding sitei415 – 4151SubstrateUniRule annotation
    Metal bindingi420 – 4201ZincUniRule annotation
    Binding sitei420 – 4201SubstrateUniRule 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

    BioCyciBJAP224911:GJEJ-1267-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:blr1256
    OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
    Taxonomic identifieri224911 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
    ProteomesiUP000002526: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 431431Histidinol dehydrogenasePRO_0000135739Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi224911.blr1256.

    Structurei

    3D structure databases

    ProteinModelPortaliP59397.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OrthoDBiEOG6CVVCR.
    PhylomeDBiP59397.

    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.

    P59397-1 [UniParc]FASTAAdd to Basket

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    MPVRLDRSSA DFDQRFAAFL AAKREVSADV EAAARAIVDD VARRGDAALL    50
    EATAKFDRLT LDASGLRVSA AEIEAAVKAC DAATLDALSL ARDRIETYHR 100
    RQLPKDERFT DPLGVELGWR YTAIESAGLY VPGGTAAYPS SVLMNAVPAK 150
    VAGVSRLVMV VPSPDGKLNP LVLAAARLGG VTEIYRVGGA QAVAALAHGT 200
    ATIAPVAKIV GPGNAYVAAA KRLVFGKVGI DMIAGPSEVL VIADDTGNAD 250
    WIAADLLAQA EHDTSAQSIL ITDSARLAAD VEKAVEAQLK TLPRTAIASA 300
    SWADFGAIIM VKNLNDAIPL ADAIAAEHLE IMTTDPDALA ARIRNAGAVF 350
    LGAHTPEAIG DYVGGSNHVL PTARSARFSS GLSVHDFMKR TSILKCGPDQ 400
    LRALGPAAMT LGKAEGLDAH SRSIGLRLNL S 431
    Length:431
    Mass (Da):44,907
    Last modified:March 25, 2003 - v1
    Checksum:i6FBB4505AD936B6D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000040 Genomic DNA. Translation: BAC46521.1.
    RefSeqiNP_767896.1. NC_004463.1.

    Genome annotation databases

    EnsemblBacteriaiBAC46521; BAC46521; BAC46521.
    GeneIDi1049433.
    KEGGibja:blr1256.
    PATRICi21186068. VBIBraJap65052_1303.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000040 Genomic DNA. Translation: BAC46521.1 .
    RefSeqi NP_767896.1. NC_004463.1.

    3D structure databases

    ProteinModelPortali P59397.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224911.blr1256.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC46521 ; BAC46521 ; BAC46521 .
    GeneIDi 1049433.
    KEGGi bja:blr1256.
    PATRICi 21186068. VBIBraJap65052_1303.

    Phylogenomic databases

    eggNOGi COG0141.
    HOGENOMi HOG000243914.
    KOi K00013.
    OrthoDBi EOG6CVVCR.
    PhylomeDBi P59397.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci BJAP224911:GJEJ-1267-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: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

    Entry informationi

    Entry nameiHISX_BRADU
    AccessioniPrimary (citable) accession number: P59397
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: March 25, 2003
    Last modified: October 1, 2014
    This is version 83 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