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)

Q7P0F6

- HISX_CHRVO

UniProt

Q7P0F6 - HISX_CHRVO

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (15 Dec 2003)
      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 sitei130 – 1301NADUniRule annotation
    Binding sitei191 – 1911NADUniRule annotation
    Binding sitei214 – 2141NADUniRule annotation
    Binding sitei237 – 2371SubstrateUniRule annotation
    Metal bindingi259 – 2591ZincUniRule annotation
    Binding sitei259 – 2591SubstrateUniRule annotation
    Metal bindingi262 – 2621ZincUniRule annotation
    Binding sitei262 – 2621SubstrateUniRule annotation
    Active sitei327 – 3271Proton acceptorUniRule annotation
    Active sitei328 – 3281Proton acceptorUniRule annotation
    Binding sitei328 – 3281SubstrateUniRule annotation
    Metal bindingi361 – 3611ZincUniRule annotation
    Binding sitei361 – 3611SubstrateUniRule annotation
    Binding sitei415 – 4151SubstrateUniRule annotation
    Metal bindingi420 – 4201ZincUniRule annotation
    Binding sitei420 – 4201SubstrateUniRule 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

    BioCyciCVIO243365:GHUD-621-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:CV_0611
    OrganismiChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
    Taxonomic identifieri243365 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium
    ProteomesiUP000001424: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 434434Histidinol dehydrogenasePRO_0000135755Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi243365.CV_0611.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7P0F6.
    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.

    Q7P0F6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLKLSSSQPD FAERLKALLA FETAQDPAVD AAVASICADV HHRGDAALVE    50
    HTNRFDRMQA AGMADLTLSR EQLEAAWLRL PADVRDALSA AAERVRRYHE 100
    KQLAHSWSYE DEDGTLLGQQ VTPLDRVGIY VPGGKAAYPS SVLMNALPAK 150
    VAGVGEIIMV VPTPGGERND LVLAAAYIAG VDKVFTVGGA QAVAALAYGT 200
    ETVPQVDKIT GPGNAYVAAA KRRVFGVVGI DMVAGPSEIL VICDGATDPD 250
    WVAMDLFSQA EHDEIAQAIL LCPSADYIAQ VEASIAKLLP SMPRRAIIEA 300
    SLAGRGALIQ VSDLAEACEI SNYIAPEHLE LSVADPDALL PQLRHAGAIF 350
    MGRFTSESLG DYCAGPNHVL PTSRTARFAS PLGVYDFQKR SSLIRVSQAG 400
    AQKLGRIASL LAHGEGLTAH ARAAELRLED GTPR 434
    Length:434
    Mass (Da):46,030
    Last modified:December 15, 2003 - v1
    Checksum:iD240002A51339F53
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016825 Genomic DNA. Translation: AAQ58287.1.
    RefSeqiNP_900281.1. NC_005085.1.
    WP_011134166.1. NC_005085.1.

    Genome annotation databases

    EnsemblBacteriaiAAQ58287; AAQ58287; CV_0611.
    GeneIDi2548270.
    KEGGicvi:CV_0611.
    PATRICi21436018. VBIChrVio67196_0610.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016825 Genomic DNA. Translation: AAQ58287.1 .
    RefSeqi NP_900281.1. NC_005085.1.
    WP_011134166.1. NC_005085.1.

    3D structure databases

    ProteinModelPortali Q7P0F6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243365.CV_0611.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAQ58287 ; AAQ58287 ; CV_0611 .
    GeneIDi 2548270.
    KEGGi cvi:CV_0611.
    PATRICi 21436018. VBIChrVio67196_0610.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci CVIO243365:GHUD-621-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 complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
      Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A.
      , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
      Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

    Entry informationi

    Entry nameiHISX_CHRVO
    AccessioniPrimary (citable) accession number: Q7P0F6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 88 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