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P59398

- HISX_BUCBP

UniProt

P59398 - HISX_BUCBP

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
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 (25 Mar 2003)
      Previous versions | rss
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    • Comment

    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 sitei131 – 1311NADUniRule annotation
    Binding sitei189 – 1891NADUniRule annotation
    Binding sitei212 – 2121NADUniRule annotation
    Binding sitei238 – 2381SubstrateUniRule annotation
    Metal bindingi260 – 2601ZincUniRule annotation
    Binding sitei260 – 2601SubstrateUniRule annotation
    Metal bindingi263 – 2631ZincUniRule annotation
    Binding sitei263 – 2631SubstrateUniRule 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

    BioCyciBAPH224915:GJ9D-94-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:bbp_094
    OrganismiBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
    Taxonomic identifieri224915 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
    ProteomesiUP000000601: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 435435Histidinol dehydrogenasePRO_0000135743Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi224915.bbp094.

    Structurei

    3D structure databases

    ProteinModelPortaliP59398.
    SMRiP59398. Positions 6-433.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    KOiK00013.
    OMAiGFLFHAN.
    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.

    P59398-1 [UniParc]FASTAAdd to Basket

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    MEVYIPIIYW KSCSEKEKRE ILFRPVVNDN SQIKEVVKEI ITNVKNSGDK    50
    ALYDYTKTFD KIRLESIQVS YGEIVDSDSF VNEEIQKSIS VAKNNIKIFH 100
    EKQTHNVVNI EIQPGVFCRQ IIRPIQSVGL YIPGGCAPLV STVLMLAIPA 150
    KIVGCKNIIL CSPPPITKEI LYASKICGIH NIFQVGGAQA IAAMAFGTKT 200
    IPKVNKIFGP GNVYVTEAKL QINALLNDLS IDMLAGPSEI LIIADFKANA 250
    CIIASDFLSQ MEHGIYSQAI LVTPSYDLAC NVIFEINIQL KNLSRKKVIN 300
    KSLKYSRIIV TKTLLECFEI SNLYAPEHLI IQCENSNRLL VYVINAGSIF 350
    LGRWSAVASG DYVTGTNHVL PTYGSAIVNS GLTVMDFQKI ISVQKLDQQG 400
    LIDVSSSIIS LSEVERMDAH TNSIKQRLIA LQDVK 435
    Length:435
    Mass (Da):48,185
    Last modified:March 25, 2003 - v1
    Checksum:i8A2F3ED2073D73F2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016826 Genomic DNA. Translation: AAO26829.1.
    RefSeqiNP_777724.1. NC_004545.1.

    Genome annotation databases

    EnsemblBacteriaiAAO26829; AAO26829; bbp_094.
    GeneIDi1058171.
    KEGGibab:bbp094.
    PATRICi21244967. VBIBucAph80364_0091.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016826 Genomic DNA. Translation: AAO26829.1 .
    RefSeqi NP_777724.1. NC_004545.1.

    3D structure databases

    ProteinModelPortali P59398.
    SMRi P59398. Positions 6-433.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224915.bbp094.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO26829 ; AAO26829 ; bbp_094 .
    GeneIDi 1058171.
    KEGGi bab:bbp094.
    PATRICi 21244967. VBIBucAph80364_0091.

    Phylogenomic databases

    eggNOGi COG0141.
    KOi K00013.
    OMAi GFLFHAN.
    OrthoDBi EOG6CVVCR.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci BAPH224915:GJ9D-94-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: Bp.

    Entry informationi

    Entry nameiHISX_BUCBP
    AccessioniPrimary (citable) accession number: P59398
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: March 25, 2003
    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