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Q323J2

- HISX_SHIBS

UniProt

Q323J2 - HISX_SHIBS

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Shigella boydii serotype 4 (strain Sb227)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (06 Dec 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 sitei130 – 1301NADUniRule annotation
    Binding sitei188 – 1881NADUniRule annotation
    Binding sitei211 – 2111NADUniRule annotation
    Binding sitei237 – 2371SubstrateUniRule annotation
    Metal bindingi259 – 2591ZincUniRule annotation
    Binding sitei259 – 2591SubstrateUniRule annotation
    Metal bindingi262 – 2621ZincUniRule annotation
    Binding sitei262 – 2621SubstrateUniRule 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

    BioCyciSBOY300268:GJFL-843-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:SBO_0846
    OrganismiShigella boydii serotype 4 (strain Sb227)
    Taxonomic identifieri300268 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
    ProteomesiUP000007067: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 434434Histidinol dehydrogenasePRO_0000135842Add
    BLAST

    Proteomic databases

    PRIDEiQ323J2.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi300268.SBO_0846.

    Structurei

    3D structure databases

    ProteinModelPortaliQ323J2.
    SMRiQ323J2. Positions 1-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiSQDSRCV.
    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.

    Q323J2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFNTIIDWN SCTAEQQRQL LMRPAISASE SITRTVNDIL DNVKARGDEA    50
    LREYSAKFDK TTVTALKVSA EEIAAASERL SDELKQAMAV AVKNIETFHT 100
    AQKLPPVDVE TQPGVRCQQV TRPVASVGLY IPGGSAPLFS TVLMLATPAR 150
    IAGCKKVVLC SPPPIADEIL YAAQLCGVQD VFNVGGAQAI AALAFGTESV 200
    PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL VIADSGATPD 250
    FVASDLLSQA EHGPDSQVIL LTPAADMARR VAEAVERQLA ELPRAETARQ 300
    ALNASRLIVT KDLAQCVEIS NQYGPEHLII QTRNARDLVD GITSAGSVFL 350
    GDWSLESAGD YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKEGF 400
    SALASTIETL AAAERLTAHK NAVTLRVNAL KEQA 434
    Length:434
    Mass (Da):46,151
    Last modified:December 6, 2005 - v1
    Checksum:i963453A026955BFF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000036 Genomic DNA. Translation: ABB65516.1.
    RefSeqiYP_407344.1. NC_007613.1.

    Genome annotation databases

    EnsemblBacteriaiABB65516; ABB65516; SBO_0846.
    GeneIDi3779803.
    KEGGisbo:SBO_0846.
    PATRICi18680408. VBIShiBoy33460_1148.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000036 Genomic DNA. Translation: ABB65516.1 .
    RefSeqi YP_407344.1. NC_007613.1.

    3D structure databases

    ProteinModelPortali Q323J2.
    SMRi Q323J2. Positions 1-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 300268.SBO_0846.

    Proteomic databases

    PRIDEi Q323J2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB65516 ; ABB65516 ; SBO_0846 .
    GeneIDi 3779803.
    KEGGi sbo:SBO_0846.
    PATRICi 18680408. VBIShiBoy33460_1148.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci SBOY300268:GJFL-843-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: Sb227.

    Entry informationi

    Entry nameiHISX_SHIBS
    AccessioniPrimary (citable) accession number: Q323J2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 64 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