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A9HFM4

- A9HFM4_GLUDA

UniProt

A9HFM4 - A9HFM4_GLUDA

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (05 Feb 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 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

    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

    BioCyciGDIA272568:GJPS-1464-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 annotationImported
    Ordered Locus Names:GDI1440Imported, Gdia_2140Imported
    OrganismiGluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5)Imported
    Taxonomic identifieri272568 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconacetobacter
    ProteomesiUP000000736: Chromosome

    Interactioni

    Protein-protein interaction databases

    STRINGi272568.GDI_1440.

    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.

    A9HFM4-1 [UniParc]FASTAAdd to Basket

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    MKRLDTAQPD FRAAFARLLD DREGDTARVD APVAEILAAV RARGDEALCA    50
    YTARFDRMPV TPDRLRITEA EIEAACARVP PDLLAALDVA ATRIEAFHRA 100
    QMPADLRYTD ADGVDLGMRW TALDAVGLYV PGGTAAYPSS VLMNAMPARV 150
    AGAARLAMCV PTPDGVLNPL VLAAARRAGV TEIYRVGGAQ AVAAMAYGTA 200
    TIRPVDRVVG PGNAYVAEAK RQVFGRVGID SIAGPSEVVV VADSGTDPRI 250
    VALDLLAQAE HDALAQSILI TQDATLADRV AEAVEAELRT LPRAAIAGAS 300
    WGAHGAIITV RDLDEAASLI DAIAPEHLEL LLADPEPLFA RVRHAGAIFL 350
    GRQCAEAIGD YVGGPNHVLP TSRTARFASG LSVFDFLKRT TFIGAGPDAL 400
    RRIGPAAVAL ARAEGLDAHA LSVSARLDAV ARESDKA 437
    Length:437
    Mass (Da):45,822
    Last modified:February 5, 2008 - v1
    Checksum:i64E29B040A3D94A7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001189 Genomic DNA. Translation: ACI51898.1.
    AM889285 Genomic DNA. Translation: CAP55383.1.
    RefSeqiYP_001601696.1. NC_010125.1.
    YP_002276513.1. NC_011365.1.

    Genome annotation databases

    EnsemblBacteriaiACI51898; ACI51898; Gdia_2140.
    CAP55383; CAP55383; GDI1440.
    GeneIDi5791558.
    6975568.
    KEGGigdi:GDI_1440.
    gdj:Gdia_2140.
    PATRICi22052716. VBIGluDia203729_2139.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001189 Genomic DNA. Translation: ACI51898.1 .
    AM889285 Genomic DNA. Translation: CAP55383.1 .
    RefSeqi YP_001601696.1. NC_010125.1.
    YP_002276513.1. NC_011365.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272568.GDI_1440.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACI51898 ; ACI51898 ; Gdia_2140 .
    CAP55383 ; CAP55383 ; GDI1440 .
    GeneIDi 5791558.
    6975568.
    KEGGi gdi:GDI_1440.
    gdj:Gdia_2140.
    PATRICi 22052716. VBIGluDia203729_2139.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci GDIA272568:GJPS-1464-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.
      Strain: PAl 5Imported.
    2. "Complete genome sequence of the sugarcane nitrogen-fixing endophyte Gluconacetobacter diazotrophicus Pal5."
      Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A., Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V., Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.
      , Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F., Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L., Figueiredo D., Montano H., Junior J., de Souza Filho G., Martin Quintana Flores V., Ferreira B., Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T., Rael Pereira A., Silva R., Rondinelli E., von Kruger W., Martins O., Baldani J.I., Ferreira P.C.
      BMC Genomics 10:450-450(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: PAl 5Imported.
    3. "Two genome sequences of the same bacterial strain, Gluconacetobacter diazotrophicus PAl 5, suggest a new standard in genome sequence submission."
      Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.
      Stand. Genomic Sci. 2:309-317(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 49037 / DSM 5601 / PAl5Imported and PAl 5Imported.

    Entry informationi

    Entry nameiA9HFM4_GLUDA
    AccessioniPrimary (citable) accession number: A9HFM4
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 5, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 62 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