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Q87QL1

- HISX_VIBPA

UniProt

Q87QL1 - HISX_VIBPA

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (06 Jun 2003)
      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 sitei127 – 1271NADUniRule annotation
    Binding sitei185 – 1851NADUniRule annotation
    Binding sitei208 – 2081NADUniRule annotation
    Binding sitei234 – 2341SubstrateUniRule annotation
    Metal bindingi256 – 2561ZincUniRule annotation
    Binding sitei256 – 2561SubstrateUniRule annotation
    Metal bindingi259 – 2591ZincUniRule annotation
    Binding sitei259 – 2591SubstrateUniRule annotation
    Active sitei323 – 3231Proton acceptorUniRule annotation
    Active sitei324 – 3241Proton acceptorUniRule annotation
    Binding sitei324 – 3241SubstrateUniRule annotation
    Metal bindingi357 – 3571ZincUniRule annotation
    Binding sitei357 – 3571SubstrateUniRule annotation
    Binding sitei411 – 4111SubstrateUniRule annotation
    Metal bindingi416 – 4161ZincUniRule annotation
    Binding sitei416 – 4161SubstrateUniRule 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

    BioCyciVPAR223926:GHK4-1187-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:VP1138
    OrganismiVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
    Taxonomic identifieri223926 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000002493: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 431431Histidinol dehydrogenasePRO_0000135876Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi223926.VP1138.

    Structurei

    3D structure databases

    ProteinModelPortaliQ87QL1.
    SMRiQ87QL1. Positions 6-429.
    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.

    Q87QL1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRTVVWQSLS EEQQDAILER PAIAEGANIT AAVADVIAKV RTQGDAALLE    50
    LTEKFDRVKP ESIRVPSKEI NAASERLSAE MKQALEQAYS NIAKFHKAQK 100
    PQPIKVETQP GVMCEQVTRP IQKVGLYIPG GSAPLPSTVL MLGVPAKIAG 150
    CRKVVLCSPP PIADEILYVA KLCGIDEVYN VGGGQAVAAM AYGTKSVSKV 200
    DKIFGPGNAY VTEAKRQVSN DFRGAAIDMP AGPSEVLVIA DETADPDFIA 250
    ADLLSQAEHG PDSQVVLVTP SPIVADQVTD AVQRQLKALS RADIAQKALA 300
    SSLIIISESI TQAVSISNYY GPEHLIVQTK NPRELLPLLD NAGSIFLGDW 350
    SPESAGDYAS GTNHVLPTYG YTRTYSSLGL ADFSKRMTVQ ELSAEGLQNL 400
    APTVVTMAEA EGLDAHKRAV TIRVEKLTQN R 431
    Length:431
    Mass (Da):46,099
    Last modified:June 6, 2003 - v1
    Checksum:iD909E8885AF3DC93
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000031 Genomic DNA. Translation: BAC59401.1.
    RefSeqiNP_797517.1. NC_004603.1.

    Genome annotation databases

    EnsemblBacteriaiBAC59401; BAC59401; BAC59401.
    GeneIDi1188643.
    KEGGivpa:VP1138.
    PATRICi20140486. VBIVibPar50997_1080.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000031 Genomic DNA. Translation: BAC59401.1 .
    RefSeqi NP_797517.1. NC_004603.1.

    3D structure databases

    ProteinModelPortali Q87QL1.
    SMRi Q87QL1. Positions 6-429.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 223926.VP1138.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC59401 ; BAC59401 ; BAC59401 .
    GeneIDi 1188643.
    KEGGi vpa:VP1138.
    PATRICi 20140486. VBIVibPar50997_1080.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci VPAR223926:GHK4-1187-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 Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
      Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
      Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RIMD 2210633.

    Entry informationi

    Entry nameiHISX_VIBPA
    AccessioniPrimary (citable) accession number: Q87QL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2003
    Last sequence update: June 6, 2003
    Last modified: October 1, 2014
    This is version 83 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