ID   SAHH_CATRO              Reviewed;         485 AA.
AC   P35007;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   02-SEP-2026, entry version 115.
DE   RecName: Full=Adenosylhomocysteinase;
DE            Short=AdoHcyase;
DE            EC=3.13.2.1;
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase;
GN   Name=SAHH;
OS   Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC   Catharanthinae; Catharanthus.
OX   NCBI_TaxID=4058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8165255; DOI=10.1104/pp.104.3.1099;
RA   Schroeder G., Waitz A., Hotze M., Schroeder J.;
RT   "cDNA for S-adenosyl-L-homocysteine hydrolase from Catharanthus roseus.";
RL   Plant Physiol. 104:1099-1100(1994).
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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine;
CC         Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1;
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC       Note=Binds 1 NAD(+) per subunit.;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- INDUCTION: By stress.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000305}.
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DR   EMBL; Z26881; CAA81527.1; -; mRNA.
DR   PIR; S38379; S38379.
DR   AlphaFoldDB; P35007; -.
DR   SMR; P35007; -.
DR   UniPathway; UPA00314; UER00076.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033353; P:L-methionine cycle; IEA:TreeGrafter.
DR   CDD; cd00401; SAHH; 1.
DR   FunFam; 3.40.50.720:FF:000004; Adenosylhomocysteinase; 1.
DR   Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   NCBIfam; TIGR00936; ahcY; 1.
DR   NCBIfam; NF004005; PRK05476.2-3; 1.
DR   PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR   PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 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; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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; Stress response.
FT   CHAIN           1..485
FT                   /note="Adenosylhomocysteinase"
FT                   /id="PRO_0000116922"
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;  53233 MW;  50CC0E99A9F66C51 CRC64;
     MALLVEKTSS GREYKVKDMS QADFGRLEIE LAEVEMPGLM SCRAEFGPSQ PFKGAKITGS
     LHMTIQTAVL IETLTALGAE VRWCSCNIFS TQEHAAAAIA RDSAAVFAWK GETLQEYWWC
     TERALDWGPD GGPDLIVDDG GDATLLIHEG VKAEEEYKKN GALPDPSSTD NAEFQIVLTI
     IRDGLKSDPT KYTRMKERLV GVSEETTTGV KRLYQMQANG TLLFPAINVN DSVTKSKFDN
     LYGCRHSLPD GLMRATDVMI AGKVAVVAGY GDVGKGCAAA LKQAGARVIV TEIDPICALQ
     ATMEGLQVLT LEDVVSEADI FVTTTGNKDI IMVDHMRKMK NNAIVCNIGH FDNEIDMLGL
     ETYPGVKRIT IKPQTDRWVF PDTNSGIIVL AEGRLMNLGC ATGHPSFVMS CSFTNQVIAQ
     LELWNERKTG KYEKKVYVLP KHLDEKVAAL HLGKLGAKLT KLTKDQADYI SVPIEGPYKP
     AHYRY
//