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Q8NNT5

- HISX_CORGL

UniProt

Q8NNT5 - HISX_CORGL

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      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 sitei129 – 1291NADUniRule annotation
    Binding sitei193 – 1931NADUniRule annotation
    Binding sitei218 – 2181NADUniRule annotation
    Binding sitei241 – 2411SubstrateUniRule annotation
    Metal bindingi263 – 2631ZincUniRule annotation
    Binding sitei263 – 2631SubstrateUniRule annotation
    Metal bindingi266 – 2661ZincUniRule annotation
    Binding sitei266 – 2661SubstrateUniRule 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:Cgl2102, cg2305
    OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
    Taxonomic identifieri196627 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
    ProteomesiUP000000582: Chromosome, UP000001009: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 442442Histidinol dehydrogenasePRO_0000135761Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi196627.cg2305.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8NNT5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiQKSLHAV.
    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.

    Q8NNT5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLNVTDLRGQ TPSKSDIRRA LPRGGTDVWS VLPIVQPVVE DVQNRGAEAA    50
    LDYGEKFDHI RPASVRVPAE VIAAAENTLD PLVRESIEES IRRVRKVHAE 100
    QKPSEHTTEL SPGGTVTERF MPIDRVGLYV PGGNAVYPSS VIMNTVPAQE 150
    AGVNSLVVAS PPQAEHGGWP HPTILAACSI LGVDEVWAVG GGQAVALLAY 200
    GDDAAGLEPV DMITGPGNIF VTAAKRLVRG VVGTDSEAGP TEIAVLADAS 250
    ANAVNVAYDL ISQAEHDVMA ASVLITDSEQ LAKDVNREIE ARYSITRNAE 300
    RVAEALRGAQ SGIVLVDDIS VGIQVADQYA AEHLEIHTEN ARAVAEQITN 350
    AGAIFVGDFS PVPLGDYSAG SNHVLPTSGS ARFSAGLSTH TFLRPVNLIE 400
    YDEAALKDVS QVVINFANAE DLPAHGEAIR ARFENLPTTD EA 442
    Length:442
    Mass (Da):46,771
    Last modified:October 1, 2002 - v1
    Checksum:iD696294519F95838
    GO

    Sequence cautioni

    The sequence AAF80392.1 differs from that shown. Reason: Frameshift at positions 97, 136 and 147.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti372 – 3809Missing1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF160480 Genomic DNA. Translation: AAF80392.1. Frameshift.
    BA000036 Genomic DNA. Translation: BAB99495.1.
    BX927154 Genomic DNA. Translation: CAF20438.1.
    RefSeqiNP_601301.1. NC_003450.3.
    YP_226339.1. NC_006958.1.

    Genome annotation databases

    EnsemblBacteriaiBAB99495; BAB99495; BAB99495.
    CAF20438; CAF20438; cg2305.
    GeneIDi1020053.
    KEGGicgb:cg2305.
    cgl:NCgl2021.
    PATRICi21496206. VBICorGlu203724_2039.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF160480 Genomic DNA. Translation: AAF80392.1 . Frameshift.
    BA000036 Genomic DNA. Translation: BAB99495.1 .
    BX927154 Genomic DNA. Translation: CAF20438.1 .
    RefSeqi NP_601301.1. NC_003450.3.
    YP_226339.1. NC_006958.1.

    3D structure databases

    ProteinModelPortali Q8NNT5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 196627.cg2305.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB99495 ; BAB99495 ; BAB99495 .
    CAF20438 ; CAF20438 ; cg2305 .
    GeneIDi 1020053.
    KEGGi cgb:cg2305.
    cgl:NCgl2021.
    PATRICi 21496206. VBICorGlu203724_2039.

    Phylogenomic databases

    eggNOGi COG0141.
    HOGENOMi HOG000243914.
    KOi K00013.
    OMAi QKSLHAV.
    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. "Molecular cloning of hisD gene from Corynebacterium glutamicum."
      Chun J.Y., Han M.S., Sim J.K., Lee M.-S.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
    2. "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
      Ikeda M., Nakagawa S.
      Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

    Entry informationi

    Entry nameiHISX_CORGL
    AccessioniPrimary (citable) accession number: Q8NNT5
    Secondary accession number(s): Q9KJU2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 90 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