Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9X0D1

- HISX_THEMA

UniProt

Q9X0D1 - HISX_THEMA

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei232 – 2321SubstrateUniRule annotation
    Metal bindingi254 – 2541ZincUniRule annotation
    Binding sitei254 – 2541SubstrateUniRule annotation
    Metal bindingi257 – 2571ZincUniRule annotation
    Binding sitei257 – 2571SubstrateUniRule annotation
    Active sitei324 – 3241Proton acceptorUniRule annotation
    Active sitei325 – 3251Proton acceptorUniRule annotation
    Binding sitei325 – 3251SubstrateUniRule annotation
    Metal bindingi358 – 3581ZincUniRule annotation
    Binding sitei358 – 3581SubstrateUniRule annotation
    Binding sitei412 – 4121SubstrateUniRule annotation
    Metal bindingi417 – 4171ZincUniRule annotation
    Binding sitei417 – 4171SubstrateUniRule 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

    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:TM_1041
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000008183: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428Histidinol dehydrogenasePRO_0000135869Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi243274.TM1041.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9X0D1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    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.

    Q9X0D1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MILMNNPGDK EVLRLLKQRM ESVSQVEETV KEIIRRVKEE GDRALEEFLK    50
    RFEKHPVGIE NLRVTEKEIS EAQVEEEFVE TIKIVIEDLK EFHRRQEERS 100
    FFFTTKGGSF LGEMVVPLES VGIYVPGGKV PYFSTLLMCA VPAIVAGVER 150
    IAVTTPPNEN GGISPYILKT CEILGLKEIY RMGGAHAVAA LTYGTETVKP 200
    VDKIVGPGGV FVTLAKKHVY GDVGIDSIAG PSEIAIVTDG SADLDLIAAD 250
    FLSQAEHDEN AMSVVITTSK EVFEKLPQVI ERHLEALPEE RRKTARISTE 300
    NFGTIILTDS LKRAFEISNL IAPEHLEVLV ENPFEPLGHI KNAGSVFLGK 350
    YTCESVGDYG AGPNHVLPTF RSARFSSGLR VSDFTKKIFI THLSEEDFRR 400
    KSELYSKMAR WEGFEAHARA IDVRREKL 428
    Length:428
    Mass (Da):47,749
    Last modified:November 1, 1999 - v1
    Checksum:iA7A765F2C298B45C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36118.1.
    PIRiH72304.
    RefSeqiNP_228847.1. NC_000853.1.
    YP_007977394.1. NC_021214.1.
    YP_008991863.1. NC_023151.1.

    Genome annotation databases

    EnsemblBacteriaiAAD36118; AAD36118; TM_1041.
    GeneIDi897023.
    KEGGitma:TM1041.
    tmi:THEMA_09155.
    tmm:Tmari_1045.
    PATRICi23937011. VBITheMar51294_1054.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36118.1 .
    PIRi H72304.
    RefSeqi NP_228847.1. NC_000853.1.
    YP_007977394.1. NC_021214.1.
    YP_008991863.1. NC_023151.1.

    3D structure databases

    ProteinModelPortali Q9X0D1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243274.TM1041.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD36118 ; AAD36118 ; TM_1041 .
    GeneIDi 897023.
    KEGGi tma:TM1041.
    tmi:THEMA_09155.
    tmm:Tmari_1045.
    PATRICi 23937011. VBITheMar51294_1054.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .

    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 43589 / MSB8 / DSM 3109 / JCM 10099.

    Entry informationi

    Entry nameiHISX_THEMA
    AccessioniPrimary (citable) accession number: Q9X0D1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 98 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