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Q39YP7

- HISX_GEOMG

UniProt

Q39YP7 - HISX_GEOMG

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (22 Nov 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 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

    BioCyciGMET269799:GHNY-384-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:Gmet_0384
    OrganismiGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)
    Taxonomic identifieri269799 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter
    ProteomesiUP000007073: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 436436Histidinol dehydrogenasePRO_0000229857Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi269799.Gmet_0384.

    Structurei

    3D structure databases

    ProteinModelPortaliQ39YP7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    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.

    Q39YP7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFLDIRDTN FDMEFAAILA RGEETGREVE QVVLDIIADV RARGDEALLE    50
    YTRRFDRLEA DSVASLQVTE DEVDYAFARV KDEEIAALKL AVERVARFHE 100
    KQKQETWLST GEPDILLGQM VTPLERVGIY VPGGKASYPS SVIMNAVPAR 150
    VAGVGEVVMV APTPGGEINP HVLVAARFSG VDRIFRLGGA QAVAALAYGT 200
    ATVPKVDKIT GPGNIYVATA KKLVFGQVGI DMIAGPSEIL VINDGSGTPA 250
    HIAADLLSQA EHDELASSIL ITTDRGFGER VAAEVERQLA ELSRETIARR 300
    SWETYGAVIV AGSLDEAIAF SNRIAPEHLE LAVTNPFDVL PKIRNAGAIF 350
    LGHFTPEAAG DYLAGPNHTL PTGGTARFFS PLSVDDFVKK SSIVYFSESG 400
    LNRLGGGIVR IAELEGLEAH GRSVSVRLKG EGEARK 436
    Length:436
    Mass (Da):46,819
    Last modified:November 22, 2005 - v1
    Checksum:i8351D95E512B3904
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000148 Genomic DNA. Translation: ABB30627.1.
    RefSeqiWP_004512356.1. NC_007517.1.
    YP_006719347.1. NC_007517.1.

    Genome annotation databases

    EnsemblBacteriaiABB30627; ABB30627; Gmet_0384.
    GeneIDi3739750.
    KEGGigme:Gmet_0384.
    PATRICi21999916. VBIGeoMet55070_0405.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000148 Genomic DNA. Translation: ABB30627.1 .
    RefSeqi WP_004512356.1. NC_007517.1.
    YP_006719347.1. NC_007517.1.

    3D structure databases

    ProteinModelPortali Q39YP7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 269799.Gmet_0384.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB30627 ; ABB30627 ; Gmet_0384 .
    GeneIDi 3739750.
    KEGGi gme:Gmet_0384.
    PATRICi 21999916. VBIGeoMet55070_0405.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci GMET269799:GHNY-384-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. "Complete sequence of Geobacter metallireducens GS-15."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
      Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: GS-15 / ATCC 53774 / DSM 7210.

    Entry informationi

    Entry nameiHISX_GEOMG
    AccessioniPrimary (citable) accession number: Q39YP7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: November 22, 2005
    Last modified: October 1, 2014
    This is version 66 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