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P10370

- HISX_SALTY

UniProt

P10370 - HISX_SALTY

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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.

    Catalytic activityi

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

    Cofactori

    Binds 1 zinc ion per subunit. At high pH manganese can replace zinc.1 Publication

    Enzyme regulationi

    Activity is lost when the metal is removed through urea denaturation or chelation, and can be regained by addition of metal.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei130 – 1301NADBy similarity
    Binding sitei188 – 1881NADBy similarity
    Binding sitei211 – 2111NADBy similarity
    Binding sitei237 – 2371SubstrateBy similarity
    Metal bindingi259 – 2591ZincBy similarity
    Binding sitei259 – 2591SubstrateBy similarity
    Metal bindingi262 – 2621ZincCurated
    Binding sitei262 – 2621SubstrateBy similarity
    Active sitei326 – 3261Proton acceptorBy similarity
    Active sitei327 – 3271Proton acceptorBy similarity
    Binding sitei327 – 3271SubstrateBy similarity
    Metal bindingi360 – 3601ZincBy similarity
    Binding sitei360 – 3601SubstrateBy similarity
    Binding sitei414 – 4141SubstrateBy similarity
    Metal bindingi419 – 4191ZincCurated
    Binding sitei419 – 4191SubstrateBy 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

    Manganese, Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-2084-MONOMER.
    SABIO-RKP10370.
    UniPathwayiUPA00031; UER00014.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidinol dehydrogenase (EC:1.1.1.23)
    Short name:
    HDH
    Gene namesi
    Name:hisD
    Ordered Locus Names:STM2072
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi99 – 991H → N: Slight decrease in activity. 1 Publication
    Mutagenesisi117 – 1171C → A or S: Almost no change in activity. 1 Publication
    Mutagenesisi154 – 1541C → A or S: Almost no change in activity. 1 Publication
    Mutagenesisi262 – 2621H → N: 7000-fold decrease in activity. 1 Publication
    Mutagenesisi327 – 3271H → N: 500-fold decrease in activity. 1 Publication
    Mutagenesisi367 – 3671H → N: Slight decrease in activity. 1 Publication
    Mutagenesisi419 – 4191H → Q: 20-fold decrease in activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 434433Histidinol dehydrogenasePRO_0000135840Add
    BLAST

    Proteomic databases

    PRIDEiP10370.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi99287.STM2072.

    Structurei

    3D structure databases

    ProteinModelPortaliP10370.
    SMRiP10370. Positions 1-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.Curated

    Phylogenomic databases

    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiYAAKLCG.
    OrthoDBiEOG6CVVCR.
    PhylomeDBiP10370.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P10370-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFNTLIDWN SCSPEQQRAL LTRPAISASD SITRTVSDIL DNVKTRGDDA    50
    LREYSAKFDK TEVTALRVTP EEIAAAGARL SDELKQAMTA AVKNIETFHS 100
    AQTLPPVDVE TQPGVRCQQV TRPVSSVGLY IPGGSAPLFS TVLMLATPAR 150
    IAGCQKVVLC SPPPIADEIL YAAQLCGVQE IFNVGGAQAI AALAFGSESV 200
    PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL VIADSGATPD 250
    FVASDLLSQA EHGPDSQVIL LTPDADIARK VAEAVERQLA ELPRADTARQ 300
    ALSASRLIVT KDLAQCVAIS NQYGPEHLII QTRNARDLVD AITSAGSVFL 350
    GDWSPESAGD YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKAGF 400
    SALASTIETL AAAERLTAHK NAVTLRVNAL KEQA 434
    Length:434
    Mass (Da):45,889
    Last modified:January 23, 2007 - v3
    Checksum:i744EDDCDAB5DF6CE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13464 Genomic DNA. Translation: CAA31823.1.
    J01804 Genomic DNA. Translation: AAA88615.1.
    AE006468 Genomic DNA. Translation: AAL20976.1.
    PIRiJS0157. DEEBHT.
    RefSeqiNP_461017.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL20976; AAL20976; STM2072.
    GeneIDi1253593.
    KEGGistm:STM2072.
    PATRICi32382727. VBISalEnt20916_2194.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13464 Genomic DNA. Translation: CAA31823.1 .
    J01804 Genomic DNA. Translation: AAA88615.1 .
    AE006468 Genomic DNA. Translation: AAL20976.1 .
    PIRi JS0157. DEEBHT.
    RefSeqi NP_461017.1. NC_003197.1.

    3D structure databases

    ProteinModelPortali P10370.
    SMRi P10370. Positions 1-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM2072.

    Proteomic databases

    PRIDEi P10370.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL20976 ; AAL20976 ; STM2072 .
    GeneIDi 1253593.
    KEGGi stm:STM2072.
    PATRICi 32382727. VBISalEnt20916_2194.

    Phylogenomic databases

    HOGENOMi HOG000243914.
    KOi K00013.
    OMAi YAAKLCG.
    OrthoDBi EOG6CVVCR.
    PhylomeDBi P10370.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci SENT99287:GCTI-2084-MONOMER.
    SABIO-RK P10370.

    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. "Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons."
      Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.
      J. Mol. Biol. 203:585-606(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: LT2.
    2. Barnes W.M., Husson R.N., Whittier R.
      Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: LT2.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    4. "Conserved cysteine residues of histidinol dehydrogenase are not involved in catalysis. Novel chemistry required for enzymatic aldehyde oxidation."
      Teng H., Segura E., Grubmeyer C.
      J. Biol. Chem. 268:14182-14188(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-15, MUTAGENESIS OF CYS-117 AND CYS-154.
    5. "The catalytically active form of histidinol dehydrogenase from Salmonella typhimurium."
      Buerger E., Goerisch H., Lingens F.
      Biochem. J. 181:771-774(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
      Strain: LT2.
    6. "A cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase."
      Grubmeyer C.T., Gray W.R.
      Biochemistry 25:4778-4784(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY ACTIVE SITE.
    7. Cited for: COFACTOR.
    8. "Mutagenesis of histidinol dehydrogenase reveals roles for conserved histidine residues."
      Teng H., Grubmeyer C.
      Biochemistry 38:7363-7371(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-99; HIS-262; HIS-327; HIS-367 AND HIS-419.

    Entry informationi

    Entry nameiHISX_SALTY
    AccessioniPrimary (citable) accession number: P10370
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 128 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    PubMed:3533140 originally reported Cys-117 to be the active site. PubMed:8314784 has shown this to be wrong.Curated

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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