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Q2YPB8

- HISX_BRUA2

UniProt

Q2YPB8 - HISX_BRUA2

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Brucella abortus (strain 2308)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (07 Feb 2006)
      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

    BioCyciBABO359391:GKDV-290-MONOMER.
    BMEL359391:GJOQ-290-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:BAB1_0285
    OrganismiBrucella abortus (strain 2308)
    Taxonomic identifieri359391 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
    ProteomesiUP000002719: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 430430Histidinol dehydrogenasePRO_0000229851Add
    BLAST

    Proteomic databases

    PRIDEiQ2YPB8.

    Interactioni

    Protein-protein interaction databases

    STRINGi359391.BAB1_0285.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2YPB8.
    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.

    Q2YPB8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVTTLRQTDP DFEQKFAAFL SGKREVSEDV DRAVREIVDR VRREGDSALL    50
    DYSRRFDRID LEKTGIAVTE AEIDAAFDAA PASTVEALKL ARDRIEKHHA 100
    RQLPKDDRYT DALGVELGSR WTAIEAVGLY VPGGTASYPS SVLMNAMPAK 150
    VAGVDRIVMV VPAPDGNLNP LVLVAARLAG VSEIYRVGGA QAIAALAYGT 200
    ETIRPVAKIV GPGNAYVAAA KRIVFGTVGI DMIAGPSEVL IVADKDNNPD 250
    WIAADLLAQA EHDMAAQSIL MTNDEAFAHA VEEAVERQLH TLARTETASA 300
    SWRDFGAVIL VKDFEDAIPL ANRIAAEHLE IAVADAEAFV PRIRNAGSIF 350
    IGGYTPEVIG DYVGGCNHVL PTARSARFSS GLSVLDYMKR TSLLKLGSEQ 400
    LRALGPAAIE IARAEGLDAH AQSVAIRLNL 430
    Length:430
    Mass (Da):46,102
    Last modified:February 7, 2006 - v1
    Checksum:i43B836B46DDF3580
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM040264 Genomic DNA. Translation: CAJ10241.1.
    RefSeqiYP_413759.1. NC_007618.1.

    Genome annotation databases

    EnsemblBacteriaiCAJ10241; CAJ10241; BAB1_0285.
    GeneIDi3788752.
    KEGGibmf:BAB1_0285.
    PATRICi17843419. VBIBruMel86222_0297.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM040264 Genomic DNA. Translation: CAJ10241.1 .
    RefSeqi YP_413759.1. NC_007618.1.

    3D structure databases

    ProteinModelPortali Q2YPB8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 359391.BAB1_0285.

    Proteomic databases

    PRIDEi Q2YPB8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAJ10241 ; CAJ10241 ; BAB1_0285 .
    GeneIDi 3788752.
    KEGGi bmf:BAB1_0285.
    PATRICi 17843419. VBIBruMel86222_0297.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci BABO359391:GKDV-290-MONOMER.
    BMEL359391:GJOQ-290-MONOMER.

    Miscellaneous databases

    PROi Q2YPB8.

    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: 2308.

    Entry informationi

    Entry nameiHISX_BRUA2
    AccessioniPrimary (citable) accession number: Q2YPB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: February 7, 2006
    Last modified: October 1, 2014
    This is version 60 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. Brucella abortus strain 2308
      Brucella abortus (strain 2308): entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3