{PDOC00603}
{PS00738; ADOHCYASE_1}
{PS00739; ADOHCYASE_2}
{BEGIN}
**************************************************
* S-adenosyl-L-homocysteine hydrolase signatures *
**************************************************

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.

-Consensus pattern: [GSAP]-[CS]-N-x-[FYLM]-S-[ST]-[QALKHD]-[DENG]-x-[AV]-
                    [AVTS]-[ADERQ]-[ACSG]-[LIVMCG]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [GA]-[KSR]-x(3)-[LIV]-x-G-[FY]-G-x-[VC]-G-[KRL]-[GA]-
                    x(1,2)-[ASC]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: April 2006 / Pattern revised.

[ 1] Sganga M.W., Aksamit R.R., Cantoni G.L., Bauer C.E.
     "Mutational and nucleotide sequence analysis of
     S-adenosyl-L-homocysteine hydrolase from Rhodobacter capsulatus."
     Proc. Natl. Acad. Sci. U.S.A. 89:6328-6332(1992).
     PubMed=1631127

--------------------------------------------------------------------------------
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html
--------------------------------------------------------------------------------

{END}