ID   SAHH_PHASS              Reviewed;         485 AA.
AC   P50249;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Adenosylhomocysteinase;
DE            Short=AdoHcyase;
DE            EC=3.3.1.1;
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase;
GN   Name=SAHH;
OS   Phalaenopsis sp. (Moth orchid).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Vandeae; Aeridinae; Phalaenopsis;
OC   unclassified Phalaenopsis.
OX   NCBI_TaxID=36900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7872785; DOI=10.1006/abbi.1995.1154;
RA   Preisig-Mueller R., Gnau P., Kindl H.;
RT   "The inducible 9, 10-dihydrophenanthrene pathway: characterization and
RT   expression of bibenzyl synthase and S-adenosylhomocysteine hydrolase.";
RL   Arch. Biochem. Biophys. 317:201-207(1995).
CC   -!- FUNCTION: Adenosylhomocysteine is a competitive inhibitor of S-
CC       adenosyl-L-methionine-dependent methyl transferase reactions; therefore
CC       adenosylhomocysteinase may play a key role in the control of
CC       methylations via regulation of the intracellular concentration of
CC       adenosylhomocysteine. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC         Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.3.1.1;
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC   -!- INDUCTION: By infection with B.cinerea.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000305}.
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DR   EMBL; X79905; CAA56278.1; -; mRNA.
DR   PIR; S71621; S71621.
DR   AlphaFoldDB; P50249; -.
DR   SMR; P50249; -.
DR   PRIDE; P50249; -.
DR   UniPathway; UPA00314; UER00076.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00401; SAHH; 1.
DR   Gene3D; 3.40.50.1480; -; 1.
DR   HAMAP; MF_00563; AdoHcyase; 1.
DR   InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR   InterPro; IPR000043; Adenosylhomocysteinase-like.
DR   InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR   PANTHER; PTHR23420; PTHR23420; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
DR   Pfam; PF00670; AdoHcyase_NAD; 1.
DR   PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1.
DR   SMART; SM00996; AdoHcyase; 1.
DR   SMART; SM00997; AdoHcyase_NAD; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00936; ahcY; 1.
DR   PROSITE; PS00738; ADOHCYASE_1; 1.
DR   PROSITE; PS00739; ADOHCYASE_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; NAD; One-carbon metabolism.
FT   CHAIN           1..485
FT                   /note="Adenosylhomocysteinase"
FT                   /id="PRO_0000116929"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         206..208
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         240
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         269..274
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         348..350
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         397
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   485 AA;  53141 MW;  1EB2CA5AD63AF233 CRC64;
     MALLVEKTTS GREYKVKDLS QADFGRLEIE LAEVEMPGLM ACRAEFGPSQ PFKGARISGS
     LHMTIQTAVL IETLTALGAE VRWCSCNIFS TQDHAAAAIA RDSAAVFAWK GETLQEYWWC
     TERCLEWGAG GGPDLIVDDG GDATLLIHEG VKAEEEYEKN GKIPDPASTD NAEFQIVLGL
     IRDSLSVDPK KYRRMKERLV GVSEETTTGV KRLYQMQYSG TLLFPAINVN DSVTKSKFDN
     LYGCRHSLPD GLMRATDVMI AGKVAVVCGY GDVGLGCAAA LKTAGARVIV TEIDPICALQ
     ALMEGLPVLR LEDVVSEADI FVTTTGNKDI IMVDHMRKMK NNAIVCNIGH FDNEIDMLGL
     ESFPGVKRIT IKPQTDRRVF PDTNSGILVL AEGRLMNLGC ATGHPSFVMS SSFTNQVIAQ
     LELWKERASG KYEKKVYVLP KHLDEKVAAL HLGKLGAKLT KLTPSQADYI SVPVEGPYKP
     AHYRY