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Q46WL2

- HISX_CUPPJ

UniProt

Q46WL2 - HISX_CUPPJ

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (13 Sep 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 sitei144 – 1441NADUniRule annotation
    Binding sitei205 – 2051NADUniRule annotation
    Binding sitei228 – 2281NADUniRule annotation
    Binding sitei251 – 2511SubstrateUniRule annotation
    Metal bindingi273 – 2731ZincUniRule annotation
    Binding sitei273 – 2731SubstrateUniRule annotation
    Metal bindingi276 – 2761ZincUniRule annotation
    Binding sitei276 – 2761SubstrateUniRule annotation
    Active sitei341 – 3411Proton acceptorUniRule annotation
    Active sitei342 – 3421Proton acceptorUniRule annotation
    Binding sitei342 – 3421SubstrateUniRule annotation
    Metal bindingi375 – 3751ZincUniRule annotation
    Binding sitei375 – 3751SubstrateUniRule annotation
    Binding sitei429 – 4291SubstrateUniRule annotation
    Metal bindingi434 – 4341ZincUniRule annotation
    Binding sitei434 – 4341SubstrateUniRule 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

    BioCyciCPIN264198:GIW3-3165-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:Reut_A3111
    OrganismiCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
    Taxonomic identifieri264198 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    ProteomesiUP000002697: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 445445Histidinol dehydrogenasePRO_0000135826Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi264198.Reut_A3111.

    Structurei

    3D structure databases

    ProteinModelPortaliQ46WL2.
    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.

    Q46WL2-1 [UniParc]FASTAAdd to Basket

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    MNATEMENVS IRRLDSSDPR FAQALREVLA FEAGEDEAID RAVAQILADV    50
    KDRGDAAVLE YTQRFDRVEA ASMGALEISQ SELEAALEDL EPKRRAALEA 100
    AAARVRAYHE KQKIECGSHS WEYTEADGTM LGQKVTPLDR VGIYVPGGKA 150
    AYPSSVLMNA IPARVAGVKE IIMVVPTPGG VRNELVLAAA QIAGVDRVFT 200
    IGGAQAVGAL AYGTATLPQV DKIVGPGNAY VAAAKRRVFG TVGIDMIAGP 250
    SEILVICDGT TDPDWVAMDL FSQAEHDELA QSILLCPDAD YIAQVEASIQ 300
    RQLDSMPRRE VIAASISGRG ALIKVRDMEE ACEIANAIAP EHLEISAENP 350
    RQWSEKIRHA GAIFLGRYTS ESLGDYCAGP NHVLPTSRTA RFSSPLGVYD 400
    FQKRSSLIEV SEGGAQMLGQ IAAELAYGEG LQAHARSAEY RFKRS 445
    Length:445
    Mass (Da):47,888
    Last modified:September 13, 2005 - v1
    Checksum:i4E3DF54A378ADE4B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000090 Genomic DNA. Translation: AAZ62471.1.
    RefSeqiYP_297315.1. NC_007347.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ62471; AAZ62471; Reut_A3111.
    GeneIDi3611937.
    KEGGireu:Reut_A3111.
    PATRICi20231936. VBIRalEut24049_3794.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000090 Genomic DNA. Translation: AAZ62471.1 .
    RefSeqi YP_297315.1. NC_007347.1.

    3D structure databases

    ProteinModelPortali Q46WL2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 264198.Reut_A3111.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ62471 ; AAZ62471 ; Reut_A3111 .
    GeneIDi 3611937.
    KEGGi reu:Reut_A3111.
    PATRICi 20231936. VBIRalEut24049_3794.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci CPIN264198:GIW3-3165-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 sequence of chromosome 1 of Ralstonia eutropha JMP134."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JMP134 / LMG 1197.

    Entry informationi

    Entry nameiHISX_CUPPJ
    AccessioniPrimary (citable) accession number: Q46WL2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 66 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3