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Q47AL5

- HISX_DECAR

UniProt

Q47AL5 - HISX_DECAR

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Dechloromonas aromatica (strain RCB)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (13 Sep 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 sitei133 – 1331NADUniRule annotation
    Binding sitei194 – 1941NADUniRule annotation
    Binding sitei217 – 2171NADUniRule annotation
    Binding sitei240 – 2401SubstrateUniRule annotation
    Metal bindingi262 – 2621ZincUniRule annotation
    Binding sitei262 – 2621SubstrateUniRule annotation
    Metal bindingi265 – 2651ZincUniRule annotation
    Binding sitei265 – 2651SubstrateUniRule annotation
    Active sitei330 – 3301Proton acceptorUniRule annotation
    Active sitei331 – 3311Proton acceptorUniRule annotation
    Binding sitei331 – 3311SubstrateUniRule annotation
    Metal bindingi364 – 3641ZincUniRule annotation
    Binding sitei364 – 3641SubstrateUniRule annotation
    Binding sitei418 – 4181SubstrateUniRule annotation
    Metal bindingi423 – 4231ZincUniRule annotation
    Binding sitei423 – 4231SubstrateUniRule 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

    BioCyciDARO159087:GI5B-3462-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:Daro_3387
    OrganismiDechloromonas aromatica (strain RCB)
    Taxonomic identifieri159087 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas
    ProteomesiUP000000550: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 433433Histidinol dehydrogenasePRO_0000135763Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi159087.Daro_3387.

    Structurei

    3D structure databases

    ProteinModelPortaliQ47AL5.
    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.

    Q47AL5-1 [UniParc]FASTAAdd to Basket

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    MVAIKRLATV DADFKAQMDA LLAFEAAQDE GIERTVIGIL ADVKARGDAA    50
    VVEYSNKFDR LTASSMADLE LSKAEMQKAL DGLPADQRQA LEAAAHRVRV 100
    YHEKQRMEGW SYTEADGTML GQMITPLDRV GLYVPGGKAA YPSSVLMNAI 150
    PAKVAGVKEL IMVVPTPGGE HNQLVLAAAC LAGVDRVFTI GGAQAVGALA 200
    YGTEAVPQVD KIVGPGNAYV ACAKRRVFGI VGIDMIAGPS EILVVADGSS 250
    DPDWVAMDLF SQAEHDELAQ SILICTDAAY IDRVQASIEK LLPTMPRREV 300
    IETSLTNRGA LILVRDLEEA CAIANRVAPE HLELSLADPD PWVAKIHHAG 350
    AIFIGHYTSE SLGDYCAGPN HVLPTSGSAR FSSPLGVYDF QKRTSLIKVS 400
    KAGAQTLGKI ASTLAHGEGL PAHAKSAEFR LEN 433
    Length:433
    Mass (Da):46,066
    Last modified:September 13, 2005 - v1
    Checksum:iA7E2E5E5990A7CCA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000089 Genomic DNA. Translation: AAZ48116.1.
    RefSeqiYP_286586.1. NC_007298.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ48116; AAZ48116; Daro_3387.
    GeneIDi3567117.
    KEGGidar:Daro_3387.
    PATRICi21605458. VBIDecAro89105_3372.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000089 Genomic DNA. Translation: AAZ48116.1 .
    RefSeqi YP_286586.1. NC_007298.1.

    3D structure databases

    ProteinModelPortali Q47AL5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 159087.Daro_3387.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ48116 ; AAZ48116 ; Daro_3387 .
    GeneIDi 3567117.
    KEGGi dar:Daro_3387.
    PATRICi 21605458. VBIDecAro89105_3372.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci DARO159087:GI5B-3462-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. "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
      Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
      BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RCB.

    Entry informationi

    Entry nameiHISX_DECAR
    AccessioniPrimary (citable) accession number: Q47AL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 68 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