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Q5LUS2

- HISX2_RUEPO

UniProt

Q5LUS2 - HISX2_RUEPO

Protein

Histidinol dehydrogenase 2

Gene

hisD2

Organism
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 Feb 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 sitei119 – 1191NADUniRule annotation
    Binding sitei181 – 1811NADUniRule annotation
    Binding sitei204 – 2041NADUniRule annotation
    Binding sitei227 – 2271SubstrateUniRule annotation
    Metal bindingi249 – 2491ZincUniRule annotation
    Binding sitei249 – 2491SubstrateUniRule annotation
    Metal bindingi252 – 2521ZincUniRule annotation
    Binding sitei252 – 2521SubstrateUniRule annotation
    Active sitei319 – 3191Proton acceptorUniRule annotation
    Active sitei320 – 3201Proton acceptorUniRule annotation
    Binding sitei320 – 3201SubstrateUniRule annotation
    Metal bindingi353 – 3531ZincUniRule annotation
    Binding sitei353 – 3531SubstrateUniRule annotation
    Binding sitei407 – 4071SubstrateUniRule annotation
    Metal bindingi412 – 4121ZincUniRule annotation
    Binding sitei412 – 4121SubstrateUniRule 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

    UniPathwayiUPA00031; UER00014.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidinol dehydrogenase 2UniRule annotation (EC:1.1.1.23UniRule annotation)
    Short name:
    HDH 2UniRule annotation
    Gene namesi
    Name:hisD2UniRule annotation
    Ordered Locus Names:SPO0981
    OrganismiRuegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
    Taxonomic identifieri246200 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria
    ProteomesiUP000001023: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 433433Histidinol dehydrogenase 2PRO_0000135847Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi246200.SPO0981.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5LUS2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK15509.
    OMAiIFIVADE.
    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.

    Q5LUS2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTITVLKSAP GLPPAPQGDA ADVVQVMLAR LRAEGEAAAR DYAARLDGWS    50
    GEIVVSPDQV ARASEQVPED LKTQIRYAHD NIRRFAEAQR ASALDFQTEL 100
    RPGLIAGQKQ IPLAAAGAYV PGGRYAHIAS ALMSIATARA AGVGQITAVS 150
    PPQVGRGVHP AILYAMSLAG ADRILALGGV QGVAALAFGL FGAPPADILV 200
    GPGNQFVAEA KRQLFGPVGI DMFAGPTDSL VIADSTADPL TVAWDLVGQA 250
    EHGYNSPVWL VTDSAALAEA VLAHIPGCIA DLPEPNRSSA QAAWDALGEV 300
    ILCTDREEMA ATADRYAPEH LHVQAADLDW WRGRLSAYGS LFLGELTTVA 350
    FGDKASGPNH VLPTSGAARY TGGLSVHKFL KTVTWQQVAP QALPDLARAT 400
    ATISRAEGME GHARTADIRL EKLRPTLRQV GTG 433
    Length:433
    Mass (Da):45,353
    Last modified:February 1, 2005 - v1
    Checksum:iB67DC5531FADA3A3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000031 Genomic DNA. Translation: AAV94285.1.
    RefSeqiYP_166233.1. NC_003911.12.

    Genome annotation databases

    EnsemblBacteriaiAAV94285; AAV94285; SPO0981.
    GeneIDi3193830.
    KEGGisil:SPO0981.
    PATRICi23375249. VBIRuePom114501_0996.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000031 Genomic DNA. Translation: AAV94285.1 .
    RefSeqi YP_166233.1. NC_003911.12.

    3D structure databases

    ProteinModelPortali Q5LUS2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 246200.SPO0981.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV94285 ; AAV94285 ; SPO0981 .
    GeneIDi 3193830.
    KEGGi sil:SPO0981.
    PATRICi 23375249. VBIRuePom114501_0996.

    Phylogenomic databases

    eggNOGi COG0141.
    HOGENOMi HOG000243914.
    KOi K15509.
    OMAi IFIVADE.
    OrthoDBi EOG6CVVCR.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .

    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 700808 / DSM 15171 / DSS-3.

    Entry informationi

    Entry nameiHISX2_RUEPO
    AccessioniPrimary (citable) accession number: Q5LUS2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 72 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