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)

Q7V004

- HISX_PROMP

UniProt

Q7V004 - HISX_PROMP

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Oct 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 sitei127 – 1271NADUniRule annotation
    Binding sitei189 – 1891NADUniRule annotation
    Binding sitei212 – 2121NADUniRule annotation
    Binding sitei235 – 2351SubstrateUniRule annotation
    Metal bindingi257 – 2571ZincUniRule annotation
    Binding sitei257 – 2571SubstrateUniRule annotation
    Metal bindingi260 – 2601ZincUniRule annotation
    Binding sitei260 – 2601SubstrateUniRule annotation
    Active sitei325 – 3251Proton acceptorUniRule annotation
    Active sitei326 – 3261Proton acceptorUniRule annotation
    Binding sitei326 – 3261SubstrateUniRule annotation
    Metal bindingi359 – 3591ZincUniRule annotation
    Binding sitei359 – 3591SubstrateUniRule annotation
    Binding sitei413 – 4131SubstrateUniRule annotation
    Metal bindingi418 – 4181ZincUniRule annotation
    Binding sitei418 – 4181SubstrateUniRule 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

    BioCyciPMAR59919:GJMQ-1528-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:PMM1488
    OrganismiProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4)
    Taxonomic identifieri59919 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
    ProteomesiUP000001026: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428Histidinol dehydrogenasePRO_0000135816Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi59919.PMM1488.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7V004.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiETFMKHS.
    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.

    Q7V004-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKIINSKQKA LQELRRISQR TTSGDNKKIN SIVENILQEV KFHGDIAVEK    50
    YTKKFDGFYP KPMQVSTRDL KTAWEETDQH LKKSLEVAYQ RIKKFHEKEI 100
    PESFTIKGEF GDSVQRRWMP VKNAGLYIPG GRAAYPSTVL MNAIPAKVAG 150
    VKEISMVSPG NEKGKINTTV LAAAYLSGVD KVFRIGGAQA IGALAFGTKQ 200
    INKVDVISGP GNIYVTTAKK LIYGFTGIDS LAGPSEILII ADRTANSSQI 250
    ASDLLAQAEH DPLASSILLT TSNDQAQEVF DEVFKIIENH PRKEICIQSI 300
    KNWGLIAICE NLESCVELSN EFAPEHLEII TIDPKTTLKS IENAGAIFLG 350
    KWTPEAVGDY LAGPNHTLPT CGNARFSGSL GVETFMKNSS IIEFNEKSLK 400
    INSVDIINLA NSEGLHSHAN SVKIRFED 428
    Length:428
    Mass (Da):47,022
    Last modified:October 1, 2003 - v1
    Checksum:i2037539E408759D6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX548174 Genomic DNA. Translation: CAE19947.1.
    RefSeqiNP_893605.1. NC_005072.1.
    WP_011133116.1. NC_005072.1.

    Genome annotation databases

    EnsemblBacteriaiCAE19947; CAE19947; PMM1488.
    GeneIDi1725608.
    KEGGipmm:PMM1488.
    PATRICi23034154. VBIProMar68066_1730.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX548174 Genomic DNA. Translation: CAE19947.1 .
    RefSeqi NP_893605.1. NC_005072.1.
    WP_011133116.1. NC_005072.1.

    3D structure databases

    ProteinModelPortali Q7V004.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 59919.PMM1488.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAE19947 ; CAE19947 ; PMM1488 .
    GeneIDi 1725608.
    KEGGi pmm:PMM1488.
    PATRICi 23034154. VBIProMar68066_1730.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci PMAR59919:GJMQ-1528-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: CCMP1986 / MED4.

    Entry informationi

    Entry nameiHISX_PROMP
    AccessioniPrimary (citable) accession number: Q7V004
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 81 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