Histidinol dehydrogenase

Details

Name
Histidinol dehydrogenase
Synonyms
  • 1.1.1.23
  • HDH
Gene Name
hisD
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011249|Histidinol dehydrogenase
MSFNTIIDWNSCTAEQQRQLLMRPAISASESITRTVNDILDNVKARGDEALREYSAKFDK
TTVTALKVSAEEIAAASERLSDELKQAMAVAVKNIETFHTAQKLPPVDVETQPGVRCQQV
TRPVASVGLYIPGGSAPLFSTVLMLATPASIAGCKKVVLCSPPPIADEILYAAQLCGVQD
VFNVGGAQAIAALAFGTESVPKVDKIFGPGNAFVTEAKRQVSQRLDGAAIDMPAGPSEVL
VIADSGATPDFVASDLLSQAEHGPDSQVILLTPAADMARRVAEAVERQLAELPRAETARQ
ALNASRLIVTKDLAQCVEISNQYGPEHLIIQTRNARELVDSITSAGSVFLGDWSPESAGD
YASGTNHVLPTYGYTATCSSLGLADFQKRMTVQELSKEGFSALASTIETLAAAERLTAHK
NAVTLRVNALKEQA
Number of residues
434
Molecular Weight
46109.815
Theoretical pI
4.81
GO Classification
Functions
histidinol dehydrogenase activity / manganese ion binding / metal ion binding / NAD binding / zinc ion binding
Processes
histidine biosynthetic process
Components
cytosol
General Function
Zinc ion binding
Specific Function
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011250|Histidinol dehydrogenase (hisD)
ATGAGCTTTAACACAATCATTGACTGGAATAGCTGTACTGCGGAGCAACAACGCCAGCTG
TTAATGCGCCCGGCGATTTCCGCCTCTGAAAGCATTACCCGCACTGTTAACGATATTCTC
GATAACGTGAAAGCACGCGGCGATGAGGCCCTGCGGGAATACAGCGCGAAGTTTGATAAA
ACCACGGTTACCGCGCTGAAGGTGTCTGCAGAGGAGATCGCCGCCGCCAGCGAACGCCTG
AGCGACGAGCTAAAACAGGCGATGGCGGTGGCAGTAAAGAATATTGAAACCTTCCACACT
GCGCAAAAACTGCCGCCGGTAGATGTAGAAACGCAGCCAGGCGTGCGTTGCCAGCAGGTC
ACGCGTCCGGTAGCTTCAGTTGGGTTGTATATTCCTGGCGGCTCCGCCCCGCTCTTCTCA
ACGGTATTAATGCTGGCGACTCCGGCGAGTATTGCGGGCTGTAAAAAAGTGGTGCTGTGC
TCACCGCCGCCGATTGCCGATGAGATCCTTTATGCGGCGCAGCTGTGCGGTGTGCAGGAC
GTGTTTAACGTCGGCGGCGCACAGGCCATTGCCGCACTGGCGTTTGGTACGGAATCTGTG
CCAAAAGTGGACAAAATCTTCGGGCCGGGTAACGCCTTTGTCACCGAAGCGAAACGTCAG
GTGAGCCAGCGTCTGGACGGTGCGGCGATCGATATGCCCGCAGGCCCGTCGGAAGTGCTG
GTGATTGCTGACAGCGGCGCTACGCCGGATTTCGTGGCTTCTGATTTGCTCTCTCAGGCT
GAACACGGCCCGGACTCACAGGTGATTTTACTGACGCCCGCTGCTGATATGGCGCGTCGC
GTTGCCGAGGCCGTCGAACGCCAACTGGCAGAACTGCCGCGTGCCGAAACCGCCCGCCAG
GCACTGAACGCCAGCCGCCTGATCGTGACTAAAGATTTAGCGCAGTGCGTGGAGATCTCC
AACCAGTACGGCCCGGAGCACCTGATCATTCAGACCCGCAACGCCCGTGAACTGGTCGAT
AGCATCACCAGCGCCGGTTCGGTATTTCTTGGTGACTGGTCACCGGAATCGGCAGGTGAT
TACGCCTCCGGCACCAACCACGTTCTACCGACTTACGGTTACACCGCCACCTGTTCCAGC
CTCGGGCTGGCAGATTTCCAGAAGCGCATGACCGTACAGGAACTGTCGAAAGAGGGGTTC
TCCGCGCTGGCTTCAACCATAGAAACACTGGCCGCCGCCGAGCGCCTGACCGCCCACAAA
AATGCCGTTACTTTGCGTGTTAACGCCCTTAAGGAGCAAGCATGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP06988
UniProtKB Entry NameHISX_ECOLI
GenBank Protein ID41709
GenBank Gene IDX13462
General References
  1. Carlomagno MS, Chiariotti L, Alifano P, Nappo AG, Bruni CB: Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons. J Mol Biol. 1988 Oct 5;203(3):585-606. [PubMed:3062174]
  2. Chiariotti L, Alifano P, Carlomagno MS, Bruni CB: Nucleotide sequence of the Escherichia coli hisD gene and of the Escherichia coli and Salmonella typhimurium hisIE region. Mol Gen Genet. 1986 Jun;203(3):382-8. [PubMed:3018428]
  3. Jovanovic G, Kostic T, Savic DJ: Nucleotide and amino acid polymorphism in the gene for L-histidinol dehydrogenase of Escherichia coli K12. Nucleic Acids Res. 1990 Jun 25;18(12):3634. [PubMed:2194167]
  4. Itoh T, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Kasai H, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Seki Y, Horiuchi T, et al.: A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):379-92. [PubMed:9097040]
  5. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [PubMed:9278503]
  6. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [PubMed:16738553]
  7. Bruni CB, Musti AM, Frunzio R, Blasi F: Structural and physiological studies of the Escherichia coli histidine operon inserted into plasmid vectors. J Bacteriol. 1980 Apr;142(1):32-42. [PubMed:6246067]
  8. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [PubMed:9298646]
  9. Barbosa JA, Sivaraman J, Li Y, Larocque R, Matte A, Schrag JD, Cygler M: Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase. Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1859-64. Epub 2002 Feb 12. [PubMed:11842181]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03366Imidazoleexperimental, investigationalunknownDetails
DB03811HistidinolexperimentalunknownDetails
DB09462Glycerinapproved, investigationalunknownDetails
DB044471,4-DithiothreitolexperimentalunknownDetails