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| PROSITE documentation PDOC00603 |
S-adenosyl-L-homocysteine hydrolase signatures
Description:
S-adenosyl-L-homocysteine hydrolase (EC 3.3.1.1) (AdoHcyase) is an enzyme of
the activated methyl cycle, responsible for the reversible hydratation 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 [1] of about 430 to 470 amino acids.
As signature patterns, we selected two highly conserved regions. The first
pattern is located in the N-terminal section; the second is derived from a
glycine-rich region in the central part of AdoHcyase; a region thought to be
involved in NAD-binding.
Last update:
April 2006 / Pattern revised.
Technical section:
PROSITE methods (with tools and information) covered by this documentation:
| ADOHCYASE_1, PS00738; S-adenosyl-L-homocysteine hydrolase signature 1 (PATTERN) |
| Consensus pattern: |
[GSAP]-[CS]-N-x-[FYLM]-S-[ST]-[QALKHD]-[DENG]-x-[AV]-[AVTS]-[ADERQ]-[ACSG]-[LIVMCG]
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| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
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| Matching PDB structures:
1A7A 1B3R 1D4F 1K0U ... [ALL] |
| ADOHCYASE_2, PS00739; S-adenosyl-L-homocysteine hydrolase signature 2 (PATTERN) |
| Consensus pattern: |
[GA]-[KSR]-x(3)-[LIV]-x-G-[FY]-G-x-[VC]-G-[KRL]-[GA]-x(1,2)-[ASC]
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| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
|
|
|
| Matching PDB structures:
1A7A 1B3R 1D4F 1K0U ... [ALL] |
Reference:
| 1 |
Authors | Sganga M.W., Aksamit R.R., Cantoni G.L., Bauer C.E. |
| Title | Mutational and nucleotide sequence analysis of S-adenosyl-L-homocysteine hydrolase from Rhodobacter capsulatus. |
| Source | Proc. Natl. Acad. Sci. U.S.A. 89:6328-6332(1992). |
| PubMed ID | 1631127 |
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