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Q5SKC1

- HISX_THET8

UniProt

Q5SKC1 - HISX_THET8

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      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 sitei118 – 1181NADUniRule annotation
    Binding sitei176 – 1761NADUniRule annotation
    Binding sitei199 – 1991NADUniRule annotation
    Binding sitei222 – 2221SubstrateUniRule annotation
    Metal bindingi244 – 2441ZincUniRule annotation
    Binding sitei244 – 2441SubstrateUniRule annotation
    Metal bindingi247 – 2471ZincUniRule annotation
    Binding sitei247 – 2471SubstrateUniRule annotation
    Active sitei311 – 3111Proton acceptorUniRule annotation
    Active sitei312 – 3121Proton acceptorUniRule annotation
    Binding sitei312 – 3121SubstrateUniRule annotation
    Metal bindingi345 – 3451ZincUniRule annotation
    Binding sitei345 – 3451SubstrateUniRule annotation
    Binding sitei399 – 3991SubstrateUniRule annotation
    Metal bindingi404 – 4041ZincUniRule annotation
    Binding sitei404 – 4041SubstrateUniRule 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

    BioCyciTTHE300852:GH8R-752-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:TTHA0722
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000532: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 412412Histidinol dehydrogenasePRO_0000135871Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi300852.TTHA0722.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5SKC1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiYAAKLCG.
    OrthoDBiEOG6CVVCR.
    PhylomeDBiQ5SKC1.

    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.

    Q5SKC1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIYAAEEVRA RFARRGLSFD PTVEEIVRGI LEAVREEGDE ALDRFSRDLD    50
    GYPVEEVPKR AWREAYEDLD EDLRDALETA RERIEAFYRE EARGGFLRAE 100
    GGGVLAQLVR PLERVGVYVP GGSAPLLSTL LMTVVPAKVA GVREVIVASP 150
    PKVHPGVLAA AWVAGADRLF AMGGAQAIAA LAYGTGRVPR VDKIVGPGNR 200
    YVVAAKRLVY GTVGIDGLAG PTETMIIADG SASPRLLAAD LLAQAEHGPD 250
    SEPWLLSPDR ALLERVEAEL SWQLQDLPRA EVARQALEKG GLVLTKDLEE 300
    AFALANLYAP EHLSLALSDP LPWLEKVQNA GGVFLGEGSP EALGDYIAGP 350
    SHVMPTSGTA RFQGGLAVRD FLKVIPVVGL SEGAARELAK KGALLARAEG 400
    LEGHARSLDL RR 412
    Length:412
    Mass (Da):44,123
    Last modified:December 21, 2004 - v1
    Checksum:i4A4BBDC4F9027A3E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008226 Genomic DNA. Translation: BAD70545.1.
    RefSeqiYP_143988.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD70545; BAD70545; BAD70545.
    GeneIDi3170022.
    KEGGittj:TTHA0722.
    PATRICi23956419. VBITheThe93045_0715.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008226 Genomic DNA. Translation: BAD70545.1 .
    RefSeqi YP_143988.1. NC_006461.1.

    3D structure databases

    ProteinModelPortali Q5SKC1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 300852.TTHA0722.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD70545 ; BAD70545 ; BAD70545 .
    GeneIDi 3170022.
    KEGGi ttj:TTHA0722.
    PATRICi 23956419. VBITheThe93045_0715.

    Phylogenomic databases

    eggNOGi COG0141.
    HOGENOMi HOG000243914.
    KOi K00013.
    OMAi YAAKLCG.
    OrthoDBi EOG6CVVCR.
    PhylomeDBi Q5SKC1.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci TTHE300852:GH8R-752-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. "Complete genome sequence of Thermus thermophilus HB8."
      Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HB8 / ATCC 27634 / DSM 579.

    Entry informationi

    Entry nameiHISX_THET8
    AccessioniPrimary (citable) accession number: Q5SKC1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 75 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