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Q8ABA9

- HISX_BACTN

UniProt

Q8ABA9 - HISX_BACTN

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (06 Jun 2003)
      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 sitei125 – 1251NADUniRule annotation
    Binding sitei187 – 1871NADUniRule annotation
    Binding sitei210 – 2101NADUniRule annotation
    Binding sitei234 – 2341SubstrateUniRule annotation
    Metal bindingi256 – 2561ZincUniRule annotation
    Binding sitei256 – 2561SubstrateUniRule annotation
    Metal bindingi259 – 2591ZincUniRule annotation
    Binding sitei259 – 2591SubstrateUniRule annotation
    Active sitei323 – 3231Proton acceptorUniRule annotation
    Active sitei324 – 3241Proton acceptorUniRule annotation
    Binding sitei324 – 3241SubstrateUniRule annotation
    Metal bindingi357 – 3571ZincUniRule annotation
    Binding sitei357 – 3571SubstrateUniRule annotation
    Binding sitei411 – 4111SubstrateUniRule annotation
    Metal bindingi416 – 4161ZincUniRule annotation
    Binding sitei416 – 4161SubstrateUniRule 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

    BioCyciBTHE226186:GJXV-202-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:BT_0201
    OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
    Taxonomic identifieri226186 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
    ProteomesiUP000001414: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428Histidinol dehydrogenasePRO_0000135732Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi226186.BT_0201.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8ABA9.
    SMRiQ8ABA9. Positions 7-428.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    KOiK00013.
    OMAiAHERIRR.
    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.

    Q8ABA9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMKLIKYPSK EQWAELLKRP ALNTESLFDT VRTIINKVRA EGDKAVLEYE    50
    AAFDKVTLSA LTVTSEEIQK AEGLISDELK SAITLAKRNI ETFHSSQRFV 100
    GKKVETMEGV TCWQKAVGIE KVGLYIPGGT APLFSTVLML AVPAKIAGCR 150
    EIVLCTPPDK NGNIHPAILF AAQLAGVSKI FKAGGVQAIA AMAYGTESVP 200
    KVYKIFGPGN QYVTAAKQLV SLRDVAIDMP AGPSEVEVLA DASANPVFVA 250
    ADLLSQAEHG VDSQAMLITT SEKLQAEVME EVNRQLAKLP RREIAAKSLE 300
    NSKLILVKDM DEALELTNAY APEHLIVETE NYLEVAERVI NAGSVFLGSL 350
    TPESAGDYAS GTNHTLPTNG YAKAYSGVSL DSFIRKITFQ EILPQGMKVI 400
    GPAIEEMAAN ELLDAHKNAV TVRLNTLK 428
    Length:428
    Mass (Da):46,246
    Last modified:June 6, 2003 - v1
    Checksum:i3C7BEEFF3BA154D1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015928 Genomic DNA. Translation: AAO75308.1.
    RefSeqiNP_809114.1. NC_004663.1.
    WP_011107162.1. NC_004663.1.

    Genome annotation databases

    EnsemblBacteriaiAAO75308; AAO75308; BT_0201.
    GeneIDi1074912.
    KEGGibth:BT_0201.
    PATRICi21055143. VBIBacThe70966_0199.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015928 Genomic DNA. Translation: AAO75308.1 .
    RefSeqi NP_809114.1. NC_004663.1.
    WP_011107162.1. NC_004663.1.

    3D structure databases

    ProteinModelPortali Q8ABA9.
    SMRi Q8ABA9. Positions 7-428.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 226186.BT_0201.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO75308 ; AAO75308 ; BT_0201 .
    GeneIDi 1074912.
    KEGGi bth:BT_0201.
    PATRICi 21055143. VBIBacThe70966_0199.

    Phylogenomic databases

    eggNOGi COG0141.
    KOi K00013.
    OMAi AHERIRR.
    OrthoDBi EOG6CVVCR.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci BTHE226186:GJXV-202-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. "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
      Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
      Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

    Entry informationi

    Entry nameiHISX_BACTN
    AccessioniPrimary (citable) accession number: Q8ABA9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2003
    Last sequence update: June 6, 2003
    Last modified: October 1, 2014
    This is version 91 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