Histidinol dehydrogenase (P06988)

Identification
Name:Histidinol dehydrogenase
Synonyms:
  • HDH
Gene Name:hisD
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity
Specific Function:Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Histidinal + 1.0Water + 1.0NAD ↔ 1.0L-Histidine + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Histidinol + 1.0NAD ↔ 1.0L-Histidinal + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+2.0Thumb+1.0Thumb ↔ 1.0Thumb+2.0Thumb+3.0Thumb
1.0L-Histidinol + 2.0NAD + 1.0Water ↔ 1.0L-Histidine + 2.0NADH + 3.0Hydrogen ion
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Histidinal
1.0L-Histidinol + 1.0NAD → 1.0NADH + 1.0Hydrogen ion + 1.0Histidinal
ReactionCard
1.0Thumb+1.0Thumb+1.0Histidinal → 2.0Thumb+1.0Thumb+1.0L-Histidine+1.0Thumb
1.0Water + 1.0NAD + 1.0Histidinal → 2.0Hydrogen ion + 1.0NADH + 1.0L-Histidine + 1.0L-Histidine
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+2.0Thumb → 3.0Thumb+1.0Thumb+2.0Thumb
1.0Water + 1.0L-Histidinol + 2.0NAD → 3.0Hydrogen ion + 1.0L-Histidine + 2.0NADH
ReactionCard
1.0Thumb+1.0Thumb+2.0Thumb → 1.0Thumb+2.0Thumb
1.0L-Histidinol + 1.0Water + 2.0NAD → 1.0L-Histidine + 2.0NADH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21225Hydrogen ionMetaboCard
ECMDB21549L-HistidinalMetaboCard
ECMDB00177L-HistidineMetaboCard
ECMDB03431L-HistidinolMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
cation binding
histidinol dehydrogenase activity
ion binding
metal ion binding
NAD or NADH binding
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
transition metal ion binding
zinc ion binding
Process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
histidine biosynthetic process
histidine family amino acid metabolic process
histidine metabolic process
metabolic process
oxidation reduction
Gene Properties
Blattner:b2020
Gene OrientationClockwise
Centisome Percentage:45.03
Left Sequence End2089121
Right Sequence End2090425
Gene Sequence:
>1305 bp
ATGAAATTTCCCGGTAAACGTAAATCCAAACATTACTTCCCCGTAAACGCACGCGATCCG
CTGCTTCAGCAATTCCAGCCAGAAAACGAAACCAGCGCTGCCTGGGTAGTGGGTATCGAT
CAAACGCTGGTCGATATTGAAGCGAAAGTGGATGATGAATTTATTGAGCGTTATGGATTA
AGCGCCGGGCATTCACTGGTGATTGAGGATGATGTAGCCGAAGCGCTTTATCAGGAACTA
AAACAGAAAAACCTGATTACCCATCAGTTTGCGGGTGGCACCATTGGTAACACCATGCAC
AACTACTCGGTGCTCGCGGACGACCGTTCGGTGCTGCTGGGCGTCATGTGCAGCAATATT
GAAATTGGCAGTTATGCCTATCGTTACCTGTGTAACACTTCCAGCCGTACCGATCTTAAC
TATCTACAAGGCGTGGATGGCCCGATTGGTCGTTGCTTTACGCTGATTGGCGAGTCCGGG
GAACGTACCTTTGCTATCAGTCCAGGCCACATGAACCAGCTGCGGGCTGAAAGCATTCCG
GAAGATGTGATTGCCGGAGCCTCGGCACTGGTTCTCACCTCATATCTGGTGCGTTGCAAG
CCGGGTGAACCCATGCCGGAAGCAACCATGAAAGCCATTGAGTACGCGAAGAAATATAAC
GTACCGGTGGTGCTGACGCTGGGCACCAAGTTTGTCATTGCCGAGAATCCGCAGTGGTGG
CAGCAATTCCTCAAAGATCACGTCTCTATCCTTGCGATGAACGAAGATGAAGCCGAAGCG
TTGACCGGAGAAAGCGATCCGTTGTTGGCATCTGACAAGGCGCTGGACTGGGTAGATCTG
GTGCTGTGCACCGCCGGGCCAATCGGCTTGTATATGGCGGGCTTTACCGAAGACGAAGCG
AAACGTAAAACCCAGCATCCGCTGCTGCCGGGCGCTATAGCGGAATTCAACCAGTATGAG
TTTAGCCGCGCCATGCGCCACAAGGATTGCCAGAATCCGCTGCGTGTATATTCGCACATT
GCGCCGTACATGGGCGGGCCGGAAAAAATCATGAACACTAATGGAGCGGGGGATGGCGCA
TTGGCAGCGTTGCTGCATGACATTACCGCCAACAGCTACCATCGTAGCAACGTACCAAAC
TCCAGCAAACATAAATTCACCTGGTTAACTTATTCATCGTTAGCGCAGGTGTGTAAATAT
GCTAACCGTGTGAGCTATCAGGTACTGAACCAGCATTCACCTCGTTTAACGCGCGGCTTG
CCGGAGCGTGAAGACAGCCTGGAAGAGTCTTACTGGGATCGTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:434
Protein Molecular Weight:46110
Protein Theoretical pI:5
PDB File:1K75
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Histidinol dehydrogenase
MSFNTIIDWNSCTAEQQRQLLMRPAISASESITRTVNDILDNVKARGDEALREYSAKFDK
TTVTALKVSAEEIAAASERLSDELKQAMAVAVKNIETFHTAQKLPPVDVETQPGVRCQQV
TRPVASVGLYIPGGSAPLFSTVLMLATPASIAGCKKVVLCSPPPIADEILYAAQLCGVQD
VFNVGGAQAIAALAFGTESVPKVDKIFGPGNAFVTEAKRQVSQRLDGAAIDMPAGPSEVL
VIADSGATPDFVASDLLSQAEHGPDSQVILLTPAADMARRVAEAVERQLAELPRAETARQ
ALNASRLIVTKDLAQCVEISNQYGPEHLIIQTRNARELVDSITSAGSVFLGDWSPESAGD
YASGTNHVLPTYGYTATCSSLGLADFQKRMTVQELSKEGFSALASTIETLAAAERLTAHK
NAVTLRVNALKEQA
References
External Links:
ResourceLink
Uniprot ID:P06988
Uniprot Name:HISX_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674616
PDB ID:1K75
Ecogene ID:EG10447
Ecocyc:EG10447
ColiBase:b2020
Kegg Gene:b2020
EchoBASE ID:EB0442
CCDB:HISX_ECOLI
BacMap:16129961
General Reference:
  • Barbosa, J. A., Sivaraman, J., Li, Y., Larocque, R., Matte, A., Schrag, J. D., Cygler, M. (2002). "Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase." Proc Natl Acad Sci U S A 99:1859-1864. Pubmed: 11842181
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Bruni, C. B., Musti, A. M., Frunzio, R., Blasi, F. (1980). "Structural and physiological studies of the Escherichia coli histidine operon inserted into plasmid vectors." J Bacteriol 142:32-42. Pubmed: 6246067
  • Carlomagno, M. S., Chiariotti, L., Alifano, P., Nappo, A. G., Bruni, C. B. (1988). "Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons." J Mol Biol 203:585-606. Pubmed: 3062174
  • Chiariotti, L., Alifano, P., Carlomagno, M. S., Bruni, C. B. (1986). "Nucleotide sequence of the Escherichia coli hisD gene and of the Escherichia coli and Salmonella typhimurium hisIE region." Mol Gen Genet 203:382-388. Pubmed: 3018428
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • 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, a. l. .. (1996). "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 3:379-392. Pubmed: 9097040
  • Jovanovic, G., Kostic, T., Savic, D. J. (1990). "Nucleotide and amino acid polymorphism in the gene for L-histidinol dehydrogenase of Escherichia coli K12." Nucleic Acids Res 18:3634. Pubmed: 2194167
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646