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Q9RSI4

- HISX_DEIRA

UniProt

Q9RSI4 - HISX_DEIRA

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 95 (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.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 sitei135 – 1351NADUniRule annotation
    Binding sitei197 – 1971NADUniRule annotation
    Binding sitei220 – 2201NADUniRule annotation
    Binding sitei243 – 2431SubstrateUniRule annotation
    Metal bindingi265 – 2651ZincUniRule annotation
    Binding sitei265 – 2651SubstrateUniRule annotation
    Metal bindingi268 – 2681ZincUniRule annotation
    Binding sitei268 – 2681SubstrateUniRule annotation
    Active sitei334 – 3341Proton acceptorUniRule annotation
    Active sitei335 – 3351Proton acceptorUniRule annotation
    Binding sitei335 – 3351SubstrateUniRule annotation
    Metal bindingi368 – 3681ZincUniRule annotation
    Binding sitei368 – 3681SubstrateUniRule annotation
    Binding sitei422 – 4221SubstrateUniRule annotation
    Metal bindingi427 – 4271ZincUniRule annotation
    Binding sitei427 – 4271SubstrateUniRule 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

    BioCyciDRAD243230:GH46-2183-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:DR_2140
    OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
    Taxonomic identifieri243230 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
    ProteomesiUP000002524: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 436436Histidinol dehydrogenasePRO_0000135766Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi243230.DR_2140.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9RSI4.
    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.

    Q9RSI4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQVLQGAEAR AALTRTFSQI PVPDAVLSRI EQTFGERLTP EQVVERILLD    50
    VRARGDDALR DWTERLDGPR PAELEVPAAE LEAAQVAPEL HAAIRLAAER 100
    VRAFYRQQPA HGFLEHGPDG ALGQLVRPLG RVGVYVPGGL APLISTLMHT 150
    AVPAQVAGVP DIVVTTPPGK DGQVHPAILV AARELGLSRV FKVGGAQAIA 200
    ALAYGTASVP AVDKIAGPGN LFVVIAKRLV YGQTGIESLP GPTETLVVAD 250
    DSASPRYVAA DLLAQAEHNG AEPVLVSVSR ELLLAVQAEL NEQLENLPEP 300
    NRSWARDSVG ARMKVVLADS LDEALDLANL YAPEHLCLLT RDPWSLLGQV 350
    RRAGGVFVGE ASMEALGDYV AGPSHVMPTG GTARFMSPVN VRDFQNIISV 400
    VGVNEETLRR IGPAAATLAR AEGLEAHARA VESRLK 436
    Length:436
    Mass (Da):46,273
    Last modified:May 1, 2000 - v1
    Checksum:iFB3A68DF7457E6B2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000513 Genomic DNA. Translation: AAF11684.1.
    PIRiA75311.
    RefSeqiNP_295863.1. NC_001263.1.

    Genome annotation databases

    EnsemblBacteriaiAAF11684; AAF11684; DR_2140.
    GeneIDi1800305.
    KEGGidra:DR_2140.
    PATRICi21631956. VBIDeiRad64572_2363.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000513 Genomic DNA. Translation: AAF11684.1 .
    PIRi A75311.
    RefSeqi NP_295863.1. NC_001263.1.

    3D structure databases

    ProteinModelPortali Q9RSI4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243230.DR_2140.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF11684 ; AAF11684 ; DR_2140 .
    GeneIDi 1800305.
    KEGGi dra:DR_2140.
    PATRICi 21631956. VBIDeiRad64572_2363.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci DRAD243230:GH46-2183-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 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

    Entry informationi

    Entry nameiHISX_DEIRA
    AccessioniPrimary (citable) accession number: Q9RSI4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 95 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