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)

Q7VA26

- HISX_PROMA

UniProt

Q7VA26 - HISX_PROMA

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 80 (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 sitei134 – 1341NADUniRule annotation
    Binding sitei196 – 1961NADUniRule annotation
    Binding sitei219 – 2191NADUniRule annotation
    Binding sitei242 – 2421SubstrateUniRule annotation
    Metal bindingi264 – 2641ZincUniRule annotation
    Binding sitei264 – 2641SubstrateUniRule annotation
    Metal bindingi267 – 2671ZincUniRule annotation
    Binding sitei267 – 2671SubstrateUniRule annotation
    Active sitei332 – 3321Proton acceptorUniRule annotation
    Active sitei333 – 3331Proton acceptorUniRule annotation
    Binding sitei333 – 3331SubstrateUniRule annotation
    Metal bindingi366 – 3661ZincUniRule annotation
    Binding sitei366 – 3661SubstrateUniRule annotation
    Binding sitei420 – 4201SubstrateUniRule annotation
    Metal bindingi425 – 4251ZincUniRule annotation
    Binding sitei425 – 4251SubstrateUniRule 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

    BioCyciPMAR167539:GJN2-1679-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:Pro_1643
    OrganismiProchlorococcus marinus (strain SARG / CCMP1375 / SS120)
    Taxonomic identifieri167539 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
    ProteomesiUP000001420: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 440440Histidinol dehydrogenasePRO_0000135813Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi167539.Pro1643.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7VA26.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    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.

    Q7VA26-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSERKQILNC IDDPQQALIM LKRISARTSL EVQENAISSV QNILTEVKQL    50
    GDEALFRLTE KFDGFIPKPL EITPEQTLEA WEKTPTPLQE ALQLAKNRIE 100
    AFHKYQIPKD FLKEGIHGEL LGKNWSPVEK AGIYIPGGRA AYPSTVLMNA 150
    VPALVAGVNE IIMVSPAGPN GQLNRTVLAA AYIAGIKKIF RIGGAQAIGA 200
    LSYGTQTIPR VDVISGPGNL YVTLAKKLVY GQVGIDSLAG PSEVLIIADH 250
    SADVEQVATD LLAQAEHDPL AASILLTTES NLAKKINLEI ENQLKDHPRS 300
    AICRKSLKDW GLIVICKDIK SCAALSNSFA PEHLELLIEK PFEFISQIKN 350
    AGAIFLGEWS PEATGDYLAG PNHTLPTSGT ARFSSALSVE TFMKSTSIIN 400
    FNQAALNKTS AAIMELANSE GLHSHSRSIE IRRSKPSSDD 440
    Length:440
    Mass (Da):47,721
    Last modified:October 1, 2003 - v1
    Checksum:iB7150E41CA0679AF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017126 Genomic DNA. Translation: AAQ00687.1.
    RefSeqiNP_876034.1. NC_005042.1.
    WP_011125793.1. NC_005042.1.

    Genome annotation databases

    EnsemblBacteriaiAAQ00687; AAQ00687; Pro_1643.
    GeneIDi1463025.
    KEGGipma:Pro_1643.
    PATRICi23030113. VBIProMar8617_1738.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017126 Genomic DNA. Translation: AAQ00687.1 .
    RefSeqi NP_876034.1. NC_005042.1.
    WP_011125793.1. NC_005042.1.

    3D structure databases

    ProteinModelPortali Q7VA26.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 167539.Pro1643.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAQ00687 ; AAQ00687 ; Pro_1643 .
    GeneIDi 1463025.
    KEGGi pma:Pro_1643.
    PATRICi 23030113. VBIProMar8617_1738.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci PMAR167539:GJN2-1679-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: SARG / CCMP1375 / SS120.

    Entry informationi

    Entry nameiHISX_PROMA
    AccessioniPrimary (citable) accession number: Q7VA26
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 80 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