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Q5FS83

- HISX_GLUOX

UniProt

Q5FS83 - HISX_GLUOX

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (01 Mar 2005)
      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 sitei129 – 1291NADUniRule annotation
    Binding sitei190 – 1901NADUniRule annotation
    Binding sitei213 – 2131NADUniRule annotation
    Binding sitei236 – 2361SubstrateUniRule annotation
    Metal bindingi258 – 2581ZincUniRule annotation
    Binding sitei258 – 2581SubstrateUniRule annotation
    Metal bindingi261 – 2611ZincUniRule annotation
    Binding sitei261 – 2611SubstrateUniRule annotation
    Active sitei326 – 3261Proton acceptorUniRule annotation
    Active sitei327 – 3271Proton acceptorUniRule annotation
    Binding sitei327 – 3271SubstrateUniRule annotation
    Metal bindingi360 – 3601ZincUniRule annotation
    Binding sitei360 – 3601SubstrateUniRule annotation
    Binding sitei414 – 4141SubstrateUniRule annotation
    Metal bindingi419 – 4191ZincUniRule annotation
    Binding sitei419 – 4191SubstrateUniRule 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

    BioCyciGOXY290633:GHB3-989-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:GOX0991
    OrganismiGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
    Taxonomic identifieri290633 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconobacter
    ProteomesiUP000006375: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 430430Histidinol dehydrogenasePRO_0000135776Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi290633.GOX0991.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5FS83.
    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.

    Q5FS83-1 [UniParc]FASTAAdd to Basket

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    MKRLDTSAAG FSEDFATLLA ARGSDERSVA EPVRAILADV RSRGDEALCD    50
    YTARFDRLTL PAEKLRISAE EIASEAARVP ADLMDALRTA ARRIETFHAA 100
    QMPKDLDFTD EDGIRLGMRW TPLDAVGLYV PGGKAAYPSS VLMNALPARV 150
    AGVKRLAMCV PSPDGVLNPL VLAAAQLCGV EEIYRIGGAQ AVGAMAFGTD 200
    LIAPVDRIVG PGNAYVAEAK RQVFGHVGID SIAGPSEVVV VADGQNDPRL 250
    VALDLLAQAE HDEQAQAILI TTDAAFAERA AEAVRKELET LPRTAIASKS 300
    WEDHGAIIVV RSLEEAAEIV NALAPEHLEV MLDAPRDFSA MIRHAGAIFM 350
    GRYCPEAVGD YVGGPNHVLP TSRTARFASG LSVFDFIKRT TTIEADEAGL 400
    RRIGPAGVAL AKAEGLDAHA LSLSVRLEKN 430
    Length:430
    Mass (Da):45,736
    Last modified:March 1, 2005 - v1
    Checksum:iC00338F3F3F3274F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000009 Genomic DNA. Translation: AAW60763.1.
    RefSeqiWP_011252557.1. NC_006677.1.
    YP_191419.1. NC_006677.1.

    Genome annotation databases

    EnsemblBacteriaiAAW60763; AAW60763; GOX0991.
    GeneIDi3250206.
    KEGGigox:GOX0991.
    PATRICi32609758. VBIGluOxy81109_1251.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000009 Genomic DNA. Translation: AAW60763.1 .
    RefSeqi WP_011252557.1. NC_006677.1.
    YP_191419.1. NC_006677.1.

    3D structure databases

    ProteinModelPortali Q5FS83.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 290633.GOX0991.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAW60763 ; AAW60763 ; GOX0991 .
    GeneIDi 3250206.
    KEGGi gox:GOX0991.
    PATRICi 32609758. VBIGluOxy81109_1251.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci GOXY290633:GHB3-989-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. "Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
      Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
      Nat. Biotechnol. 23:195-200(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 621H.

    Entry informationi

    Entry nameiHISX_GLUOX
    AccessioniPrimary (citable) accession number: Q5FS83
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: March 1, 2005
    Last modified: October 1, 2014
    This is version 69 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