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Q3SI67

- HISX_THIDA

UniProt

Q3SI67 - HISX_THIDA

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Thiobacillus denitrificans (strain ATCC 25259)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (11 Oct 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

    BioCyciTDEN292415:GHWG-1747-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:Tbd_1713
    OrganismiThiobacillus denitrificans (strain ATCC 25259)
    Taxonomic identifieri292415 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus
    ProteomesiUP000008291: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 434434Histidinol dehydrogenasePRO_0000135872Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi292415.Tbd_1713.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3SI67.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiQKSLHAV.
    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.

    Q3SI67-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLTLTRLDSA QPDFQARLAR LLQFDDATDA SIEEAVATIL HAVKTRGDAA    50
    VLEYTERFDR LPAPSAASLE LGAAELAAAL AGLPEDTRAA LEAAADRVRR 100
    YHEKQLQGSW TYTEDDGTVL GQKVTPLDRV GLYVPGGKAA YPSSVLMNAI 150
    PAKVAGVAEL VMVVPTPGGE RNALVLAAAA IAGVDRVFTI GGAQAVAALA 200
    YGTETVPQVD KIVGPGNAYV AAAKRRVFGT VGIDMIAGPS EILVIADGST 250
    PAEWVAMDLF SQAEHDELAQ SILLSPDPDY LDAVAAAIDQ LIVEMPRAEV 300
    IRTSLTNRGA LIRTHDLHDA AAIANAIAPE HLELAVSDPE ALLPKLRHAG 350
    AIFMGKNTCE ALGDYCAGPN HVLPTSRTAR FSSPLGVYDF QKRTSLIHVS 400
    EAGAQTLGRI AATLAYGEGL QAHARSAEYR LTHK 434
    Length:434
    Mass (Da):45,762
    Last modified:October 11, 2005 - v1
    Checksum:iE319DE59B7083FC5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000116 Genomic DNA. Translation: AAZ97666.1.
    RefSeqiYP_315471.1. NC_007404.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ97666; AAZ97666; Tbd_1713.
    GeneIDi3671296.
    KEGGitbd:Tbd_1713.
    PATRICi23969587. VBIThiDen82923_1696.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000116 Genomic DNA. Translation: AAZ97666.1 .
    RefSeqi YP_315471.1. NC_007404.1.

    3D structure databases

    ProteinModelPortali Q3SI67.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 292415.Tbd_1713.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ97666 ; AAZ97666 ; Tbd_1713 .
    GeneIDi 3671296.
    KEGGi tbd:Tbd_1713.
    PATRICi 23969587. VBIThiDen82923_1696.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci TDEN292415:GHWG-1747-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. "The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans."
      Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.
      J. Bacteriol. 188:1473-1488(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25259.

    Entry informationi

    Entry nameiHISX_THIDA
    AccessioniPrimary (citable) accession number: Q3SI67
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 67 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