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Q5QWP8

- HISX_IDILO

UniProt

Q5QWP8 - HISX_IDILO

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (04 Jan 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 sitei132 – 1321NADUniRule annotation
    Binding sitei194 – 1941NADUniRule annotation
    Binding sitei217 – 2171NADUniRule annotation
    Binding sitei243 – 2431SubstrateUniRule annotation
    Metal bindingi265 – 2651ZincUniRule annotation
    Binding sitei265 – 2651SubstrateUniRule annotation
    Metal bindingi268 – 2681ZincUniRule annotation
    Binding sitei268 – 2681SubstrateUniRule annotation
    Active sitei332 – 3321Proton acceptorUniRule annotation
    Active sitei333 – 3331Proton acceptorUniRule annotation
    Binding sitei333 – 3331SubstrateUniRule annotation
    Metal bindingi366 – 3661ZincUniRule annotation
    Binding sitei366 – 3661SubstrateUniRule annotation
    Binding sitei420 – 4201SubstrateUniRule annotation
    Metal bindingi425 – 4251ZincUniRule annotation
    Binding sitei425 – 4251SubstrateUniRule 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

    BioCyciILOI283942:GI0U-1845-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:IL1835
    OrganismiIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
    Taxonomic identifieri283942 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina
    ProteomesiUP000001171: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 442442Histidinol dehydrogenasePRO_0000135781Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi283942.IL1835.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5QWP8.
    SMRiQ5QWP8. Positions 7-439.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiDEMAMPI.
    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.

    Q5QWP8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSELRIPIEQ WQSLSSAEQT QRLARPGRAQ AESLREKVAV ILSDVRDNGE    50
    RAVLNYTRQF DNPDATSLRM SDEQVEAAVA SLDDKVKRAI DTAYQTIYRF 100
    HEAQRPQDLS IETAPGVQCE LRYAPLDAVG LYIPGGSATL PSTALMLGVP 150
    AQIAGCQRVV MVSPPNKQGE LPAALLYAAK RCGVTDILLC GGAQAIGALA 200
    YGIESSPAVG KVFGPGNSFV TEAKQQVSQN DSGCAMDLPA GPSELLVIAD 250
    DSANPAYVAA DLLSQAEHGP DSQVILLTPS MTVAENVRQE LMAQCAQLSR 300
    ADIAEQALQA SRLLVVADMN EAIAISETYA PEHLSIQTDN ARDLLPQLTR 350
    AGSVFVGHYT PESGGDYATG TNHVLPTYGY ARNYSSLGLV DFYRRYTVQE 400
    ASHDGLRQLA EAITTLADVE GLDAHKRAVT IRTETKSTES KL 442
    Length:442
    Mass (Da):47,447
    Last modified:January 4, 2005 - v1
    Checksum:i45D9665DC7D9465F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017340 Genomic DNA. Translation: AAV82667.1.
    RefSeqiYP_156216.1. NC_006512.1.

    Genome annotation databases

    EnsemblBacteriaiAAV82667; AAV82667; IL1835.
    GeneIDi3173855.
    KEGGiilo:IL1835.
    PATRICi22141786. VBIIdiLoi21852_1842.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017340 Genomic DNA. Translation: AAV82667.1 .
    RefSeqi YP_156216.1. NC_006512.1.

    3D structure databases

    ProteinModelPortali Q5QWP8.
    SMRi Q5QWP8. Positions 7-439.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 283942.IL1835.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV82667 ; AAV82667 ; IL1835 .
    GeneIDi 3173855.
    KEGGi ilo:IL1835.
    PATRICi 22141786. VBIIdiLoi21852_1842.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci ILOI283942:GI0U-1845-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: ATCC BAA-735 / DSM 15497 / L2-TR.

    Entry informationi

    Entry nameiHISX_IDILO
    AccessioniPrimary (citable) accession number: Q5QWP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 73 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