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)

Q9PM77

- HISX_CAMJE

UniProt

Q9PM77 - HISX_CAMJE

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
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 (01 Oct 2000)
      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 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

    BioCyciCJEJ192222:GJTS-1557-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:Cj1598
    OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
    Taxonomic identifieri192222 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
    ProteomesiUP000000799: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428Histidinol dehydrogenasePRO_0000135751Add
    BLAST

    Proteomic databases

    PRIDEiQ9PM77.

    Interactioni

    Protein-protein interaction databases

    STRINGi192222.Cj1598.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9PM77.
    SMRiQ9PM77. Positions 3-428.
    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.

    Q9PM77-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQILVYDNLD EKQKEEALKR PAISAKDEIS KIVSSIIKEV QEKGDKALIE    50
    QALKFDKAEI SKIKITQEEI TQASNRLDKD LQEAILVAYE NIKKFHEAQI 100
    PHEIALETTK GVKCEVLTRP IEKVGLYIPG GLAPLFSTVL MLAIPAKIAG 150
    CEKIVLASPA KINDAVLFCA KLCGVDEIYQ MGGAGAIAAL TYGTQSVLKV 200
    DKIFGPGNAF VTEAKRQVSS DINGAAIDMQ AGPSEVLVIA DDLANEKFVA 250
    SDLLSQAEHG ADSQVILVCL SQDFAKKASD EVQSQLELLP RKELASKSIA 300
    NSRIIIAKDL NQALEISNLY APEHLIIQTQ NPRELLKGVK HAGSVFLGAY 350
    SPESMGDYAS GTNHVLPTYG LTKTHSSLGL ADFSKRMTVQ ELSKEGFLAL 400
    GKSVEILAQN EHLDAHKNAV TFRLESLK 428
    Length:428
    Mass (Da):46,446
    Last modified:October 1, 2000 - v1
    Checksum:i16F08561BF7DB738
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL111168 Genomic DNA. Translation: CAL35695.1.
    PIRiD81255.
    RefSeqiYP_002344967.1. NC_002163.1.

    Genome annotation databases

    EnsemblBacteriaiCAL35695; CAL35695; Cj1598.
    GeneIDi905868.
    KEGGicje:Cj1598.
    PATRICi20060156. VBICamJej33762_1574.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL111168 Genomic DNA. Translation: CAL35695.1 .
    PIRi D81255.
    RefSeqi YP_002344967.1. NC_002163.1.

    3D structure databases

    ProteinModelPortali Q9PM77.
    SMRi Q9PM77. Positions 3-428.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 192222.Cj1598.

    Proteomic databases

    PRIDEi Q9PM77.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAL35695 ; CAL35695 ; Cj1598 .
    GeneIDi 905868.
    KEGGi cje:Cj1598.
    PATRICi 20060156. VBICamJej33762_1574.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci CJEJ192222:GJTS-1557-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: NCTC 11168.

    Entry informationi

    Entry nameiHISX_CAMJE
    AccessioniPrimary (citable) accession number: Q9PM77
    Secondary accession number(s): Q0P830
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: October 1, 2000
    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