Summary: Histidinol dehydrogenase
This is the Wikipedia entry entitled "Histidinol dehydrogenase". More...
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Histidinol dehydrogenase Edit Wikipedia article
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
the l-histidinol dehydrogenase (hisd) structure implicates domain swapping and gene duplication.
- L-histidinol + 2 NAD+ L-histidine + 2 NADH + 2 H+
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-histidinol:NAD+ oxidoreductase. This enzyme is also called L-histidinol dehydrogenase.
In 4-electron dehydrogenases, a single active site catalyses 2 separate oxidation steps: oxidation of the substrate alcohol to an intermediate aldehyde; and oxidation of the aldehyde to the product acid, in this case His. The reaction proceeds via a tightly- or covalently-bound inter-mediate, and requires the presence of 2 NAD molecules. By contrast with most dehydrogenases, the substrate is bound before the NAD coenzyme. A Cys residue has been implicated in the catalytic mechanism of the second oxidative step.
In bacteria HDH is a single chain polypeptide; in fungi it is the C-terminal domain of a multifunctional enzyme which catalyses three different steps of histidine biosynthesis; and in plants it is expressed as a nuclear encoded protein precursor which is exported to the chloroplast.
- Grubmeyer CT, Gray WR (August 1986). "A cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase". Biochemistry 25 (17): 4778–84. doi:10.1021/bi00365a009. PMID 3533140.
- Nagai A, Ward E, Beck J, Tada S, Chang JY, Scheidegger A, Ryals J (May 1991). "Structural and functional conservation of histidinol dehydrogenase between plants and microbes". Proc. Natl. Acad. Sci. U.S.A. 88 (10): 4133–7. doi:10.1073/pnas.88.10.4133. PMC 51612. PMID 2034659.
- Cowan-Jacob SW, Rahuel J, Nagai A, Iwasaki G, Ohta D (November 1996). "Crystallization and preliminary crystallographic analysis of cabbage histidinol dehydrogenase". Acta Crystallogr. D Biol. Crystallogr. 52 (Pt 6): 1188–90. doi:10.1107/S0907444996008396. PMID 15299582.
- Barbosa JA, Sivaraman J, Li Y, Larocque R, Matte A, Schrag JD, Cygler M (February 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 (4): 1859–64. doi:10.1073/pnas.022476199. PMC 122284. PMID 11842181.
- Adams E (1954). "Enzymatic synthesis of histidine from histidinol". J. Biol. Chem. 209 (2): 829–846. PMID 13192138.
- Adams E (1955). "L-Histidinal, a biosynthetic precursor of histidine". J. Biol. Chem. 217 (1): 325–344. PMID 13271397.
- Yourno J, Ino I (1968). "Purification and crystallization of histidinol dehydrogenase from Salmonella typhimurium LT-2". J. Biol. Chem. 243 (12): 3273–6. PMID 4872177.
- Loper JC (1968). "Histidinol dehydrogenase from Salmonella typhimurium Crystallization and composition studies". J. Biol. Chem. 243 (12): 3264–72. PMID 4872176.
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Histidinol dehydrogenase Provide feedback
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External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR012131
Histidinol dehydrogenase (HDH) catalyzes the terminal step in the biosynthesis of histidine in bacteria, fungi, and plants, the four-electron oxidation of L-histidinol to histidine.
In 4-electron dehydrogenases, a single active site catalyses 2 separate oxidation steps: oxidation of the substrate alcohol to an intermediate aldehyde; and oxidation of the aldehyde to the product acid, in this case His [PUBMED:3533140]. The reaction proceeds via a tightly- or covalently-bound inter-mediate, and requires the presence of 2 NAD molecules [PUBMED:3533140]. By contrast with most dehydrogenases, the substrate is bound before the NAD coenzyme [PUBMED:3533140]. A Cys residue has been implicated in the catalytic mechanism of the second oxidative step [PUBMED:3533140].
In bacteria HDH is a single chain polypeptide; in fungi it is the C-terminal domain of a multifunctional enzyme which catalyzes three different steps of histidine biosynthesis; and in plants it is expressed as nuclear encoded protein precursor which is exported to the chloroplast [PUBMED:2034659].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||zinc ion binding (GO:0008270)|
|NAD binding (GO:0051287)|
|histidinol dehydrogenase activity (GO:0004399)|
|Biological process||histidine biosynthetic process (GO:0000105)|
|oxidation-reduction process (GO:0055114)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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The aldehyde dehydrogenases (ALDHs) are a superfamily of multimeric enzymes which catalyse the oxidation of a broad range of aldehydes into their corresponding carboxylic acids with the reduction of their cofactor, NAD(P) into NAD(P)H. The way that the NAD is bound is distinct from other NAD(P)-dependent oxidoreductases. The domain represented by this clan consists of two similar subdomains.
The clan contains the following 4 members:Aldedh DUF1487 Histidinol_dh LuxC
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Curation and family details
|Seed source:||Pfam-B_1358 (release 2.1)|
|Number in seed:||16|
|Number in full:||3998|
|Average length of the domain:||401.20 aa|
|Average identity of full alignment:||42 %|
|Average coverage of the sequence by the domain:||91.68 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||15|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Histidinol_dh domain has been found. There are 8 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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