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Q9RQ82

- HISX_BUCMH

UniProt

Q9RQ82 - HISX_BUCMH

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Buchnera aphidicola subsp. Melaphis rhois
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      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.By similarity

    Catalytic activityi

    L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Pathwayi

    GO - Molecular functioni

    1. histidinol dehydrogenase activity Source: UniProtKB-EC
    2. NAD binding Source: InterPro
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. histidine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00031; UER00014.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidinol dehydrogenase (EC:1.1.1.23)
    Short name:
    HDH
    Gene namesi
    Name:hisD
    OrganismiBuchnera aphidicola subsp. Melaphis rhois
    Taxonomic identifieri118103 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›201›201Histidinol dehydrogenasePRO_0000135745Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9RQ82.
    SMRiQ9RQ82. Positions 6-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.Curated

    Family and domain databases

    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR012131. Hstdl_DH.
    [Graphical view]
    PfamiPF00815. Histidinol_dh. 1 hit.
    [Graphical view]
    PRINTSiPR00083. HOLDHDRGNASE.
    SUPFAMiSSF53720. SSF53720. 1 hit.

    Sequencei

    Sequence statusi: Fragment.

    Q9RQ82-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKNCLKIIHW DRCSIEEREK ILSRPILDDL SAIKKQVKTI ISDVNSLGDQ    50
    ALYNYTNIFD KIKLNNIKIS HQDLVKAELC IDVKAKNAIQ VAIDNIRTFH 100
    ISQNISTLNI EINKGIYCQQ IVRPIGSVGL YIPGGSAPLL STVLMLAIPA 150
    RIAGCKKIVL CSPPPITNEV LYASKICGVQ EIFQVGGAQA IAALGFGTET 200
    I 201
    Length:201
    Mass (Da):22,028
    Last modified:May 1, 2000 - v1
    Checksum:iE0FA5769CF7DB395
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei201 – 2011

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF129283 Genomic DNA. Translation: AAF13776.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF129283 Genomic DNA. Translation: AAF13776.1 .

    3D structure databases

    ProteinModelPortali Q9RQ82.
    SMRi Q9RQ82. Positions 6-201.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .

    Family and domain databases

    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR012131. Hstdl_DH.
    [Graphical view ]
    Pfami PF00815. Histidinol_dh. 1 hit.
    [Graphical view ]
    PRINTSi PR00083. HOLDHDRGNASE.
    SUPFAMi SSF53720. SSF53720. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence evolution in bacterial endosymbionts having extreme base compositions."
      Clark M.A., Moran N.A., Baumann P.
      Mol. Biol. Evol. 16:1586-1598(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiHISX_BUCMH
    AccessioniPrimary (citable) accession number: Q9RQ82
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: May 1, 2000
    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

    Documents

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

    External Data

    Dasty 3