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)

B0S9F2

- HISX_LEPBA

UniProt

B0S9F2 - HISX_LEPBA

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (08 Apr 2008)
      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 sitei124 – 1241NADUniRule annotation
    Binding sitei185 – 1851NADUniRule annotation
    Binding sitei208 – 2081NADUniRule annotation
    Binding sitei233 – 2331SubstrateUniRule annotation
    Metal bindingi255 – 2551ZincUniRule annotation
    Binding sitei255 – 2551SubstrateUniRule annotation
    Metal bindingi258 – 2581ZincUniRule annotation
    Binding sitei258 – 2581SubstrateUniRule 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 bindingi418 – 4181ZincUniRule annotation
    Binding sitei418 – 4181SubstrateUniRule 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

    BioCyciLBIF355278:GHTJ-1770-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:LBF_1772
    OrganismiLeptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
    Taxonomic identifieri355278 [NCBI]
    Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
    ProteomesiUP000001846: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 430430Histidinol dehydrogenasePRO_1000135438Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi355278.LBF_1772.

    Structurei

    3D structure databases

    ProteinModelPortaliB0S9F2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    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.

    B0S9F2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPIPILHCDR NSKELYSRFL QGAREDLTTA TDRILPILES VRTQGDQALF    50
    SYTEMFDGIK LSQLTIDPKK IKTNVDEKTK EAFLRAKSNI EAFHMEQKRE 100
    SWSKVIDGNR LGVKYTPIPS LAVYAPGGKA LYPSSVLMGI IPAKIAGVPS 150
    IQLITPPQKD GIPEILVWLA QIMDIDRIVT VGGAQGIAAA AYGTESVPKS 200
    EFIVGPGNAY VAAAKSYLSG QGLIGIESPA GPSEVCIIAD ENANPKWIAC 250
    DMLSQAEHGE DSSAILLTTD LTLAKRVSEE LEIAFSERPK RLQMKQTAIY 300
    ENSSILVFPT LDDCIWFSNE LAPEHLEIQT KDYESVFAKI EHAGSVFLGP 350
    YSPVAMGDYI SGTNHILPTA RGSRIYSSLG VDTFLKRVTF QEVTKESLEN 400
    LYPFVKLMSE LEGLDEEHGT SVKVRTRQFQ 430
    Length:430
    Mass (Da):47,347
    Last modified:April 8, 2008 - v1
    Checksum:i3D0CA083966873FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000777 Genomic DNA. Translation: ABZ94279.1.
    RefSeqiWP_012388809.1. NC_010842.1.
    YP_001962857.1. NC_010842.1.

    Genome annotation databases

    EnsemblBacteriaiABZ94279; ABZ94279; LBF_1772.
    GeneIDi6387233.
    KEGGilbf:LBF_1772.
    PATRICi22342647. VBILepBif95142_1879.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000777 Genomic DNA. Translation: ABZ94279.1 .
    RefSeqi WP_012388809.1. NC_010842.1.
    YP_001962857.1. NC_010842.1.

    3D structure databases

    ProteinModelPortali B0S9F2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 355278.LBF_1772.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABZ94279 ; ABZ94279 ; LBF_1772 .
    GeneIDi 6387233.
    KEGGi lbf:LBF_1772.
    PATRICi 22342647. VBILepBif95142_1879.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci LBIF355278:GHTJ-1770-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. "Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis."
      Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A.
      , Davies J.K., Medigue C., Adler B.
      PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Patoc 1 / Ames.

    Entry informationi

    Entry nameiHISX_LEPBA
    AccessioniPrimary (citable) accession number: B0S9F2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 56 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3