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P06988

- HISX_ECOLI

UniProt

P06988 - HISX_ECOLI

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 5 (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.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei130 – 1301NAD
    Binding sitei188 – 1881NAD
    Binding sitei211 – 2111NAD
    Binding sitei237 – 2371Substrate
    Metal bindingi259 – 2591Zinc
    Binding sitei259 – 2591Substrate
    Metal bindingi262 – 2621Zinc
    Binding sitei262 – 2621Substrate
    Active sitei326 – 3261Proton acceptor
    Active sitei327 – 3271Proton acceptor
    Binding sitei327 – 3271Substrate
    Metal bindingi360 – 3601Zinc
    Binding sitei360 – 3601Substrate
    Binding sitei414 – 4141Substrate
    Metal bindingi419 – 4191Zinc
    Binding sitei419 – 4191Substrate

    GO - Molecular functioni

    1. histidinol dehydrogenase activity Source: EcoCyc
    2. manganese ion binding Source: EcoCyc
    3. metal ion binding Source: EcoCyc
    4. NAD binding Source: InterPro
    5. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. histidine biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:HISTDEHYD-MONOMER.
    ECOL316407:JW2002-MONOMER.
    MetaCyc:HISTDEHYD-MONOMER.
    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:b2020, JW2002
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10447. hisD.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 434433Histidinol dehydrogenasePRO_0000135770Add
    BLAST

    Proteomic databases

    PaxDbiP06988.
    PRIDEiP06988.

    2D gel databases

    SWISS-2DPAGEP06988.

    Expressioni

    Gene expression databases

    GenevestigatoriP06988.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    IntActiP06988. 7 interactions.
    STRINGi511145.b2020.

    Structurei

    Secondary structure

    1
    434
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 84
    Helixi9 – 113
    Helixi14 – 207
    Helixi30 – 5425
    Beta strandi57 – 593
    Beta strandi64 – 674
    Helixi70 – 7910
    Helixi82 – 10019
    Beta strandi107 – 1126
    Beta strandi115 – 1239
    Beta strandi125 – 1306
    Beta strandi134 – 1363
    Helixi140 – 15213
    Beta strandi155 – 1617
    Helixi167 – 1759
    Beta strandi180 – 1834
    Helixi186 – 19510
    Beta strandi198 – 2003
    Beta strandi204 – 2074
    Helixi212 – 22312
    Beta strandi225 – 2273
    Beta strandi229 – 2313
    Beta strandi238 – 2436
    Helixi249 – 26012
    Beta strandi267 – 2737
    Helixi275 – 28915
    Helixi295 – 3028
    Beta strandi306 – 3094
    Helixi313 – 32311
    Beta strandi326 – 3327
    Helixi335 – 3384
    Helixi339 – 3413
    Beta strandi346 – 3516
    Helixi356 – 3616
    Beta strandi363 – 3653
    Helixi374 – 3763
    Helixi383 – 3864
    Beta strandi387 – 3959
    Helixi397 – 41317
    Helixi417 – 43317

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K75X-ray1.75A/B1-434[»]
    1KAEX-ray1.70A/B1-434[»]
    1KAHX-ray2.10A/B1-434[»]
    1KARX-ray2.10A/B1-434[»]
    ProteinModelPortaliP06988.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06988.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiYAAKLCG.
    OrthoDBiEOG6CVVCR.
    PhylomeDBiP06988.

    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.

    P06988-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFNTIIDWN SCTAEQQRQL LMRPAISASE SITRTVNDIL DNVKARGDEA    50
    LREYSAKFDK TTVTALKVSA EEIAAASERL SDELKQAMAV AVKNIETFHT 100
    AQKLPPVDVE TQPGVRCQQV TRPVASVGLY IPGGSAPLFS TVLMLATPAS 150
    IAGCKKVVLC SPPPIADEIL YAAQLCGVQD VFNVGGAQAI AALAFGTESV 200
    PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL VIADSGATPD 250
    FVASDLLSQA EHGPDSQVIL LTPAADMARR VAEAVERQLA ELPRAETARQ 300
    ALNASRLIVT KDLAQCVEIS NQYGPEHLII QTRNARELVD SITSAGSVFL 350
    GDWSPESAGD YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKEGF 400
    SALASTIETL AAAERLTAHK NAVTLRVNAL KEQA 434
    Length:434
    Mass (Da):46,110
    Last modified:January 23, 2007 - v5
    Checksum:i4B4F2EA00C9BEA4E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151E → V(PubMed:3062174)Curated
    Sequence conflicti15 – 151E → V(PubMed:3018428)Curated
    Sequence conflicti22 – 221M → T in CAA27610. (PubMed:3018428)Curated
    Sequence conflicti150 – 1501S → R(PubMed:3062174)Curated
    Sequence conflicti150 – 1501S → R(PubMed:3018428)Curated
    Sequence conflicti157 – 1571V → A in CAA36882. (PubMed:2194167)Curated
    Sequence conflicti313 – 3131L → S(PubMed:3062174)Curated
    Sequence conflicti313 – 3131L → S(PubMed:3018428)Curated
    Sequence conflicti403 – 4031L → V(PubMed:3062174)Curated
    Sequence conflicti403 – 4031L → V(PubMed:3018428)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13462 Genomic DNA. Translation: CAA31812.1.
    X03972 Genomic DNA. Translation: CAA27610.1.
    X52656 Genomic DNA. Translation: CAA36882.1.
    U00096 Genomic DNA. Translation: AAC75081.1.
    AP009048 Genomic DNA. Translation: BAA15851.1.
    M10483 Genomic DNA. Translation: AAA23962.1.
    PIRiC64967. DEECHT.
    RefSeqiNP_416524.1. NC_000913.3.
    YP_490263.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75081; AAC75081; b2020.
    BAA15851; BAA15851; BAA15851.
    GeneIDi12931409.
    946531.
    KEGGiecj:Y75_p1983.
    eco:b2020.
    PATRICi32119375. VBIEscCol129921_2097.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13462 Genomic DNA. Translation: CAA31812.1 .
    X03972 Genomic DNA. Translation: CAA27610.1 .
    X52656 Genomic DNA. Translation: CAA36882.1 .
    U00096 Genomic DNA. Translation: AAC75081.1 .
    AP009048 Genomic DNA. Translation: BAA15851.1 .
    M10483 Genomic DNA. Translation: AAA23962.1 .
    PIRi C64967. DEECHT.
    RefSeqi NP_416524.1. NC_000913.3.
    YP_490263.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K75 X-ray 1.75 A/B 1-434 [» ]
    1KAE X-ray 1.70 A/B 1-434 [» ]
    1KAH X-ray 2.10 A/B 1-434 [» ]
    1KAR X-ray 2.10 A/B 1-434 [» ]
    ProteinModelPortali P06988.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P06988. 7 interactions.
    STRINGi 511145.b2020.

    2D gel databases

    SWISS-2DPAGE P06988.

    Proteomic databases

    PaxDbi P06988.
    PRIDEi P06988.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75081 ; AAC75081 ; b2020 .
    BAA15851 ; BAA15851 ; BAA15851 .
    GeneIDi 12931409.
    946531.
    KEGGi ecj:Y75_p1983.
    eco:b2020.
    PATRICi 32119375. VBIEscCol129921_2097.

    Organism-specific databases

    EchoBASEi EB0442.
    EcoGenei EG10447. hisD.

    Phylogenomic databases

    eggNOGi COG0141.
    HOGENOMi HOG000243914.
    KOi K00013.
    OMAi YAAKLCG.
    OrthoDBi EOG6CVVCR.
    PhylomeDBi P06988.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci EcoCyc:HISTDEHYD-MONOMER.
    ECOL316407:JW2002-MONOMER.
    MetaCyc:HISTDEHYD-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P06988.
    PROi P06988.

    Gene expression databases

    Genevestigatori P06988.

    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: K12.
    2. "Nucleotide sequence of the Escherichia coli hisD gene and of the Escherichia coli and Salmonella typhimurium hisIE region."
      Chiariotti L., Alifano P., Carlomagno M.S., Bruni C.B.
      Mol. Gen. Genet. 203:382-388(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Nucleotide and amino acid polymorphism in the gene for L-histidinol dehydrogenase of Escherichia coli K12."
      Savic D.J., Jovanovic G., Kostic T.
      Nucleic Acids Res. 18:3634-3634(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3100 / ATCC 14948 / DSM 6302.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. "Structural and physiological studies of the Escherichia coli histidine operon inserted into plasmid vectors."
      Bruni C.B., Musti A.M., Frunzio R., Blasi F.
      J. Bacteriol. 142:32-42(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 296-319.
    8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    9. "Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase."
      Barbosa J.A.R.G., Sivaraman J., Li Y., Larocque R., Matte A., Schrag J.D., Cygler M.
      Proc. Natl. Acad. Sci. U.S.A. 99:1859-1864(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
      Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.

    Entry informationi

    Entry nameiHISX_ECOLI
    AccessioniPrimary (citable) accession number: P06988
    Secondary accession number(s): O08506, P78076, Q47254
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 146 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3