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Q606Q2

- HISX_METCA

UniProt

Q606Q2 - HISX_METCA

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (23 Nov 2004)
      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 sitei135 – 1351NADUniRule 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

    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:MCA1963
    OrganismiMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
    Taxonomic identifieri243233 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaMethylococcalesMethylococcaceaeMethylococcus
    ProteomesiUP000006821: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 436436Histidinol dehydrogenasePRO_0000135794Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi243233.MCA1963.

    Structurei

    Secondary structure

    1
    436
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 104
    Helixi16 – 249
    Helixi32 – 4817
    Helixi50 – 6112
    Helixi68 – 714
    Helixi75 – 839
    Helixi87 – 10721
    Beta strandi112 – 1154
    Beta strandi121 – 1288
    Beta strandi130 – 1356
    Helixi144 – 15714
    Beta strandi160 – 1656
    Helixi169 – 1713
    Helixi175 – 18410
    Beta strandi188 – 1903
    Helixi194 – 20310
    Beta strandi206 – 2083
    Beta strandi212 – 2154
    Helixi220 – 22910
    Beta strandi233 – 2353
    Beta strandi243 – 2486
    Helixi254 – 26512
    Beta strandi272 – 2787
    Helixi280 – 29314
    Helixi294 – 2963
    Helixi300 – 31011
    Beta strandi312 – 3154
    Helixi319 – 32911
    Beta strandi332 – 3398
    Helixi341 – 3444
    Helixi345 – 3473
    Beta strandi352 – 3565
    Helixi380 – 3823
    Helixi389 – 3924
    Beta strandi393 – 3997

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4GICX-ray2.05A/B2-422[»]
    ProteinModelPortaliQ606Q2.
    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.

    Q606Q2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEVKIKRLY TGDADFASQL DRLLAWSESE DTDIHQRVTE IIGCIRRDGD    50
    AALVELTARF DHFVVDTAAA LELPRDVLEA AWQALPAEQA KALREAAERI 100
    RAYAERQKLD SWDYREADGT LLGQKITPLD RVGLYVPGGK AAYPSSVLMN 150
    AVPAKVAGVP ELIMAVPAPR GELNALVLAA AYISGVDRVF RIGGAQAVAA 200
    LAYGTETVPR VDKIVGPGNI YVATAKKLVF GQVGIDMVAG PSEILVISDG 250
    RTDPDWIAMD LFSQAEHDED AQAILISPDA AHLEAVQASI ERLLPGMERA 300
    EVIRTSLERR GGMILVDDLE QAAAVANRIA PEHLELSVES PEVLVESIRN 350
    AGAIFMGRYT AEALGDYCAG PNHVLPTSGT ARFSSPLGVY DFQKRSSLIY 400
    CSPDGADQLG RTASLLAWGE GLGAHARSAE YRIRHH 436
    Length:436
    Mass (Da):47,045
    Last modified:November 23, 2004 - v1
    Checksum:i161D3DEAAE8BDE17
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017282 Genomic DNA. Translation: AAU92021.1.
    RefSeqiYP_114396.1. NC_002977.6.

    Genome annotation databases

    EnsemblBacteriaiAAU92021; AAU92021; MCA1963.
    GeneIDi3102435.
    KEGGimca:MCA1963.
    PATRICi22607774. VBIMetCap22254_1995.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017282 Genomic DNA. Translation: AAU92021.1 .
    RefSeqi YP_114396.1. NC_002977.6.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4GIC X-ray 2.05 A/B 2-422 [» ]
    ProteinModelPortali Q606Q2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243233.MCA1963.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAU92021 ; AAU92021 ; MCA1963 .
    GeneIDi 3102435.
    KEGGi mca:MCA1963.
    PATRICi 22607774. VBIMetCap22254_1995.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .

    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: ATCC 33009 / NCIMB 11132 / Bath.

    Entry informationi

    Entry nameiHISX_METCA
    AccessioniPrimary (citable) accession number: Q606Q2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 74 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3