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)

P28736

- HISX_MYCSM

UniProt

P28736 - HISX_MYCSM

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Mycobacterium smegmatis
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      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.By similarity

    Catalytic activityi

    L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei136 – 1361NADBy similarity
    Binding sitei200 – 2001NADBy similarity
    Binding sitei228 – 2281NADBy similarity
    Binding sitei251 – 2511SubstrateBy similarity
    Metal bindingi273 – 2731ZincBy similarity
    Binding sitei273 – 2731SubstrateBy similarity
    Metal bindingi276 – 2761ZincBy similarity
    Binding sitei276 – 2761SubstrateBy similarity
    Active sitei342 – 3421Proton acceptorBy similarity
    Active sitei343 – 3431Proton acceptorBy similarity
    Binding sitei343 – 3431SubstrateBy similarity
    Metal bindingi376 – 3761ZincBy similarity
    Binding sitei376 – 3761SubstrateBy similarity
    Binding sitei430 – 4301SubstrateBy similarity
    Metal bindingi435 – 4351ZincBy similarity
    Binding sitei435 – 4351SubstrateBy similarity

    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 dehydrogenase (EC:1.1.1.23)
    Short name:
    HDH
    Gene namesi
    Name:hisD
    OrganismiMycobacterium smegmatis
    Taxonomic identifieri1772 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 445445Histidinol dehydrogenasePRO_0000135798Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP28736.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.Curated

    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.

    P28736-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNMMAKFQMS RIDLRNRVLS AAQLRSALPR GGVDVDAVVP KVRPIVDAVA    50
    QRGAQAALEY GESFDGIRPE TVRVPRELLS QALENLDADV RAALQVSIDR 100
    ARAVHADQRR TDTTTTLAPG ATVTERWVPV ERVGLYVPGG NAVYPSSVVM 150
    NVVPAQTAGV DSMVIASPPQ GQFGGRPHPT ILAAAALLGV DEVWAVGGAQ 200
    AVALLAYGGT DTDGAELAPV DMITGPGNIY VTAAKRICRS QVGIDAEAGP 250
    TEIAILADHT ADPVHVAADL ISQAEHDEMA ASVLVTDSET LAEATDRELA 300
    NQLATTKHVE RVTAALSGKQ SAIVLVDDID AGVRTVNAYA AEHLEIQTVD 350
    APGVAGRIRS AGAIFVGAWS PVSLGDYCAG SNHVLPTAGC ARHSSGLSVQ 400
    TFLRGIHVVE YDEAALKDVS GHVITLSKAE DLPAHGEAVR RRFER 445
    Length:445
    Mass (Da):46,703
    Last modified:December 1, 1992 - v1
    Checksum:i19996D28D4591170
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65542 Genomic DNA. Translation: CAA46509.1.
    PIRiS26209.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65542 Genomic DNA. Translation: CAA46509.1 .
    PIRi S26209.

    3D structure databases

    ProteinModelPortali P28736.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Cloning of mycobacterial histidine synthesis genes by complementation of a Mycobacterium smegmatis auxotroph."
      Hinshelwood S., Stoker N.G.
      Mol. Microbiol. 6:2887-2895(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 607 / DSM 43465 / JCM 20379 / NBRC 3207 / NRRL B-692.

    Entry informationi

    Entry nameiHISX_MYCSM
    AccessioniPrimary (citable) accession number: P28736
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3