ID   SAHH_LEIDO              Reviewed;         437 AA.
AC   P36889;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Adenosylhomocysteinase;
DE            Short=AdoHcyase;
DE            EC=3.3.1.1;
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase;
OS   Leishmania donovani.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DI700;
RX   PubMed=1501636; DOI=10.1016/0166-6851(92)90019-g;
RA   Henderson D.M., Hanson S., Allen T., Wilson K., Coulter-Karis D.E.,
RA   Greenberg M.L., Hershfield M.S., Ullman B.;
RT   "Cloning of the gene encoding Leishmania donovani S-adenosylhomocysteine
RT   hydrolase, a potential target for antiparasitic chemotherapy.";
RL   Mol. Biochem. Parasitol. 53:169-183(1992).
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=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;
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000305}.
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DR   EMBL; M76556; AAA29265.1; -; Genomic_DNA.
DR   PIR; A45569; A45569.
DR   AlphaFoldDB; P36889; -.
DR   SMR; P36889; -.
DR   VEuPathDB; TriTrypDB:LdBPK_364100.1; -.
DR   VEuPathDB; TriTrypDB:LdCL_360048000; -.
DR   VEuPathDB; TriTrypDB:LDHU3_36.5490; -.
DR   UniPathway; UPA00314; UER00076.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; -; 3.
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; 2.
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   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; NAD; One-carbon metabolism.
FT   CHAIN           1..437
FT                   /note="Adenosylhomocysteinase"
FT                   /id="PRO_0000116915"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         156..158
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         219..224
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         298..300
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   437 AA;  47792 MW;  D687C918DE2B0637 CRC64;
     MADYKVKDIS LAEWGRKAIE LAENEMPGLM ELRREYGPSQ PLKGAKIAGC LHMTVQTAVL
     IETLKALGAD VRWSSCNIFS TQDNAAAAIA KAGVPVFAWK GETDEEYEWC IAQTVKGFSG
     DGLPNMILDD GGDLTNLVID HHPELVPKIF GISEETTTGV KNLYKRLSKG NLPMCAINVN
     DSVTKSKFDN LYGCRESLVD GMKRATDVMI AGKTCCVCGY GDVGKGCAAA LRAFGARVVV
     TEVDPINALQ ASMEGYQVAL VEDVMADAHI FVTTTGNDDI ITSEHFPHMR DDAIVCNIGH
     FDTEIQVGWL EANAKEHVEI KPQVDRYTME NGRHIILLAK GRLVNLGCAS GHPSFVMSNS
     FTNQVLAQIE LWSNRDNGKY PRGDKAGVFF LPKALDEKVA ALHLAHVGAK LTKLTPKQAE
     YINCPVNGPF KPDHYRY