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Q9CLM4

- HISX_PASMU

UniProt

Q9CLM4 - HISX_PASMU

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Pasteurella multocida (strain Pm70)
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 (01 Jun 2001)
      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 sitei232 – 2321SubstrateUniRule annotation
    Metal bindingi254 – 2541ZincUniRule annotation
    Binding sitei254 – 2541SubstrateUniRule annotation
    Metal bindingi257 – 2571ZincUniRule annotation
    Binding sitei257 – 2571SubstrateUniRule annotation
    Active sitei321 – 3211Proton acceptorUniRule annotation
    Active sitei322 – 3221Proton acceptorUniRule annotation
    Binding sitei322 – 3221SubstrateUniRule annotation
    Metal bindingi355 – 3551ZincUniRule annotation
    Binding sitei355 – 3551SubstrateUniRule annotation
    Binding sitei409 – 4091SubstrateUniRule annotation
    Metal bindingi414 – 4141ZincUniRule annotation
    Binding sitei414 – 4141SubstrateUniRule 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

    BioCyciPMUL272843:GC8W-1248-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:PM1198
    OrganismiPasteurella multocida (strain Pm70)
    Taxonomic identifieri272843 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
    ProteomesiUP000000809: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428Histidinol dehydrogenasePRO_0000135808Add
    BLAST

    Proteomic databases

    PRIDEiQ9CLM4.

    Interactioni

    Protein-protein interaction databases

    STRINGi272843.PM1198.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CLM4.
    SMRiQ9CLM4. Positions 6-428.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiDEMAMPI.
    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.

    Q9CLM4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQTLIWNTLN SAQKQAALSR PAQAVGEQIT QAVNAIKSNV INNGDKALFE    50
    LAEKFDKTTL ESLVISKAQV EQASQRIATE LKQAIQTAKG NIERFHQAQK 100
    NQTVDLETQA GVRCQVVTRP IQNVGLYIPG GSAPLFSTVL MLAVPAKIAG 150
    CKTIVLCSPP PIADEILYTA NLCGVETIYA IGGAQAIFAM ANGTESVQKV 200
    DKIFGPGNAF VTEAKRQVLQ QGTAIDMPAG PSEVLVIADE FADPDFVASD 250
    LLSQAEHGSD SQVILVTNCE TLAKQTALSI EQQLARLPRA ETARKALAHS 300
    RTFIAEDLQQ CVEISNAYAP EHLVVQVENA RNLLPFLDNA GSIFLGAYSP 350
    ESMGDYASGT NHVLPTYGYT RTHSSLGLAD FSKRMTVQEL TPQGFKDLAN 400
    TVMLMAEAEQ LEAHKQAVAI RLEKLTQE 428
    Length:428
    Mass (Da):46,150
    Last modified:June 1, 2001 - v1
    Checksum:i583D332D94F1F4AF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004439 Genomic DNA. Translation: AAK03282.1.
    RefSeqiNP_246135.1. NC_002663.1.

    Genome annotation databases

    EnsemblBacteriaiAAK03282; AAK03282; PM1198.
    GeneIDi1244545.
    KEGGipmu:PM1198.
    PATRICi22871649. VBIPasMul88067_1209.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004439 Genomic DNA. Translation: AAK03282.1 .
    RefSeqi NP_246135.1. NC_002663.1.

    3D structure databases

    ProteinModelPortali Q9CLM4.
    SMRi Q9CLM4. Positions 6-428.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272843.PM1198.

    Proteomic databases

    PRIDEi Q9CLM4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK03282 ; AAK03282 ; PM1198 .
    GeneIDi 1244545.
    KEGGi pmu:PM1198.
    PATRICi 22871649. VBIPasMul88067_1209.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci PMUL272843:GC8W-1248-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Pm70.

    Entry informationi

    Entry nameiHISX_PASMU
    AccessioniPrimary (citable) accession number: Q9CLM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: June 1, 2001
    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