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Q318Q4

- HISX_PROM9

UniProt

Q318Q4 - HISX_PROM9

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Prochlorococcus marinus (strain MIT 9312)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (06 Dec 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 sitei139 – 1391NADUniRule annotation
    Binding sitei201 – 2011NADUniRule annotation
    Binding sitei224 – 2241NADUniRule annotation
    Binding sitei247 – 2471SubstrateUniRule annotation
    Metal bindingi269 – 2691ZincUniRule annotation
    Binding sitei269 – 2691SubstrateUniRule annotation
    Metal bindingi272 – 2721ZincUniRule annotation
    Binding sitei272 – 2721SubstrateUniRule annotation
    Active sitei337 – 3371Proton acceptorUniRule annotation
    Active sitei338 – 3381Proton acceptorUniRule annotation
    Binding sitei338 – 3381SubstrateUniRule annotation
    Metal bindingi371 – 3711ZincUniRule annotation
    Binding sitei371 – 3711SubstrateUniRule annotation
    Binding sitei425 – 4251SubstrateUniRule annotation
    Metal bindingi430 – 4301ZincUniRule annotation
    Binding sitei430 – 4301SubstrateUniRule 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

    BioCyciPMAR74546:GHRG-1618-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:PMT9312_1581
    OrganismiProchlorococcus marinus (strain MIT 9312)
    Taxonomic identifieri74546 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
    ProteomesiUP000002715: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 440440Histidinol dehydrogenasePRO_0000229861Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi74546.PMT9312_1581.

    Structurei

    3D structure databases

    ProteinModelPortaliQ318Q4.
    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.

    Q318Q4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGREPFNLKN LEMRIINNKK DAIQELKRIS SRTNSENNNK INLIVEEILQ    50
    EVKTYGDIAV EKYTKKFDGF NPDPMQISED HLKDAWDEID SNLKRSLEVA 100
    HKRIKKFHEK EIPQSFTIKG EHGDTVQRRW RPVKNAGIYI PGGRAAYPST 150
    VLMNAIPAKV AGVEEIIMVS PGNKEGEINK TVLAAAHLSG IKKVFRIGGA 200
    QAIGALAFGT NQINKVDVIT GPGNIYVTTA KKLIYGSTGI DSLAGPSEIL 250
    VIADETAQST HIASDLLAQA EHDPLASSIL LTTSKNQAKE VLEELYKKID 300
    DHPRKEICMQ SIKNWGLIVI CENYELCIEL SNNFAPEHLE ILALDSKKIL 350
    EGIENAGAIF LGKWTPEAVG DYLAGPNHTL PTSGNSRFSG SLGVETFMKN 400
    TSIIEFNEES LKVNSLDIIN LAESEGLHSH ANSVKIRFED 440
    Length:440
    Mass (Da):48,592
    Last modified:December 6, 2005 - v1
    Checksum:i5D93F6C85EBF6D0F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000111 Genomic DNA. Translation: ABB50641.1.
    RefSeqiWP_011377123.1. NC_007577.1.
    YP_398077.1. NC_007577.1.

    Genome annotation databases

    EnsemblBacteriaiABB50641; ABB50641; PMT9312_1581.
    GeneIDi3766398.
    KEGGipmi:PMT9312_1581.
    PATRICi23007178. VBIProMar70153_1752.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000111 Genomic DNA. Translation: ABB50641.1 .
    RefSeqi WP_011377123.1. NC_007577.1.
    YP_398077.1. NC_007577.1.

    3D structure databases

    ProteinModelPortali Q318Q4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 74546.PMT9312_1581.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB50641 ; ABB50641 ; PMT9312_1581 .
    GeneIDi 3766398.
    KEGGi pmi:PMT9312_1581.
    PATRICi 23007178. VBIProMar70153_1752.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci PMAR74546:GHRG-1618-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 Prochlorococcus marinus str. MIT 9312."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MIT 9312.

    Entry informationi

    Entry nameiHISX_PROM9
    AccessioniPrimary (citable) accession number: Q318Q4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 67 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3