AdoHcyase_NADS-adenosyl-L-homocysteine hydrolase, NAD binding domain |
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| SMART accession number: | SM00997
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| Description: |
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| Interpro abstract (IPR015878): |
S-adenosyl-L-homocysteine hydrolase (EC 3.3.1.1) (AdoHcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydration of S-adenosyl-L-homocysteine into adenosine and homocysteine. AdoHcyase is an ubiquitous enzyme which binds and requires NAD+ as a cofactor. AdoHcyase is a highly conserved protein [(PUBMED:1631127)] of about 430 to 470 amino acids. This entry represents the glycine-rich region in the central part of AdoHcyase, which is thought to be involved in NAD-binding [(PUBMED:1631127)].
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| Family alignment: |
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There are 1265
AdoHcyase_NAD domains in 1265 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Cellular role (predicted cellular role)
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Cellular role: metabolism
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Sganga MW, Aksamit RR, Cantoni GL, Bauer CE
- Mutational and nucleotide sequence analysis of S-adenosyl-L-homocysteinehydrolase from Rhodobacter capsulatus.
- Proc Natl Acad Sci U S A. 1992; 89: 6328-32
- Display abstract
The genetic locus ahcY, encoding the enzyme S-adenosyl-L-homocysteinehydrolase (EC 3.3.1.1) from the bacterium Rhodobacter capsulatus, has beenmapped by mutational analysis to within a cluster of genes involved inregulating the induction and maintenance of the bacterial photosyntheticapparatus. Sequence analysis demonstrates that ahcY encodes a 51-kDapolypeptide that displays 64% sequence identity to its human homolog.Insertion mutants in ahcY lack detectable S-adenosyl-L-homocysteinehydrolase activity and, as a consequence, S-adenosyl-L-homocysteineaccumulates in the cells, resulting in a 16-fold decrease in theintracellular ratio of S-adenosyl-L-methionine toS-adenosyl-L-homocysteine as compared to wild-type cells. The ahcYdisrupted strain fails to grow in minimal medium; however, growth isrestored in minimal medium supplemented with methionine or homocysteine orin a complex medium, thereby indicating that the hydrolysis ofS-adenosyl-L-homocysteine plays a key role in the metabolism ofsulfur-containing amino acids. The ahcY mutant, when grown in supplementedmedium, synthesizes significantly reduced levels of bacteriochlorophyll,indicating that modulation of the intracellular ratio ofS-adenosyl-L-methionine to S-adenosyl-L-homocysteine may be an importantfactor in regulating bacteriochlorophyll biosynthesis.
- Structure (3D structures containing this domain)
3D Structures of AdoHcyase_NAD domains in PDB
| PDB code | Main view | Title | | 1a7a |  | Structure of human placental s-adenosylhomocysteine hydrolase: determination of a 30 selenium atom substructure from data at a single wavelength |
| 1b3r |  | Rat liver s-adenosylhomocystein hydrolase |
| 1d4f |  | Crystal structure of recombinant rat-liver d244e mutant s- adenosylhomocysteine hydrolase |
| 1k0u |  | Inhibition of s-adenosylhomocysteine hydrolase by "acyclic sugar" adenosine analogue d-eritadenine |
| 1ky4 |  | S-adenosylhomocysteine hydrolase refined with noncrystallographic restraints |
| 1ky5 |  | D244e mutant s-adenosylhomocysteine hydrolase refined with noncrystallographic restraints |
| 1li4 |  | Human s-adenosylhomocysteine hydrolase complexed with neplanocin |
| 1v8b |  | Crystal structure of a hydrolase |
| 1xwf |  | K185n mutated s-adenosylhomocysteine hydrolase |
| 2h5l |  | S-adenosylhomocysteine hydrolase containing nad and 3-deaza- d-eritadenine |
| 2ziz |  | Crystal structure of mycobacterium tuberculosis s-adenosyl- l-homocysteine hydrolase in ternary complex with nad and 3- deazaadenosine |
| 2zj0 |  | Crystal structure of mycobacterium tuberculosis s-adenosyl- l-homocysteine hydrolase in ternary complex with nad and 2- fluoroadenosine |
| 2zj1 |  | Crystal structure of mycobacterium tuberculosis s-adenosyl- l-homocysteine hydrolase in ternary complex with nad and 3'-keto-aristeromycin |
| 3ce6 |  | Crystal structure of mycobacterium tuberculosis s-adenosyl- l-homocysteine hydrolase in ternary complex with nad and adenosine |
| 3d64 |  | Crystal structure of s-adenosyl-l-homocysteine hydrolase from burkholderia pseudomallei |
| 3dhy |  | Crystal structures of mycobacterium tuberculosis s-adenosyl- l-homocysteine hydrolase in ternary complex with substrate and inhibitors |
| 3g1u |  | Crystal structure of leishmania major s- adenosylhomocysteine hydrolase |
| 3glq |  | Crystal structure of s-adenosyl-l-homocysteine hydrolase from burkholderia pseudomallei in complex with 9-beta-d- arabino-furansyl-adenine |
| 3gvp |  | Human sahh-like domain of human adenosylhomocysteinase 3 |
| 3h9u |  | S-adenosyl homocysteine hydrolase (sahh) from trypanosoma brucei |
- Links (links to other resources describing this domain)
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to expand nodes. To display all proteins with a AdoHcyase_NAD domain in a specific node, click on it.