ID   SAHH_TRIVA              Reviewed;         486 AA.
AC   P51540;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Adenosylhomocysteinase;
DE            Short=AdoHcyase;
DE            EC=3.3.1.1;
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase;
OS   Trichomonas vaginalis.
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=5722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WAA38;
RX   PubMed=8892301; DOI=10.1016/0166-6851(96)02683-7;
RA   Bagnara A.S., Tucker V.E., Minotto L., Howes E.R., Ko G.A., Edwards M.R.,
RA   Dawes I.W.;
RT   "Molecular characterisation of adenosylhomocysteinase from Trichomonas
RT   vaginalis.";
RL   Mol. Biochem. Parasitol. 81:1-12(1996).
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; 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   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000305}.
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DR   EMBL; U40872; AAC47319.1; -; Genomic_DNA.
DR   AlphaFoldDB; P51540; -.
DR   SMR; P51540; -.
DR   STRING; 5722.XP_001325201.1; -.
DR   PRIDE; P51540; -.
DR   VEuPathDB; TrichDB:TVAG_405240; -.
DR   eggNOG; KOG1370; Eukaryota.
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   3: Inferred from homology;
KW   Hydrolase; NAD; One-carbon metabolism.
FT   CHAIN           1..486
FT                   /note="Adenosylhomocysteinase"
FT                   /id="PRO_0000116919"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         210..212
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         273..278
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         331
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         352..354
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         400
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   486 AA;  53439 MW;  1403C6750587427C CRC64;
     MACKSPAGAP FEYRIADINL HVLGRKELTL AEKEMPGLMV LRERYSASKP LKGVRISGSL
     HMTVQTAVLI ETLTALGADV RWASCNIFST QDTAAAAIVV GPTGTPEKPA GIPVFAWKGE
     TLPEYWENTY RALTWPDGQG PQQVVDDGGD ATLLISKGFE FETAGAVPEP TEADNLEYRC
     VLATLKQVFN QDKNHWHTVA AGMNGVSEET TTGVHRLYQL EKEGKLLFPA INVNDAVTKS
     KFDNIYGCRH SLIDGINRAS DVMIGGKTAL VMGYGDVGKG CAQSLRGQGA RVIITEVDPI
     CALQAVMEGY QVRRIEEVVK DVDIFVTCTG NCDIISVDMM AQMKDKAIVG NIGHFDNEID
     TDGLMKYPGI KHIPIKPEYD MWEFPDGHAI LLLAEGRLLN LGCATGHPSF VMSMSFTNQT
     LAQLDLYEKR GNLEMKVYTL PKHLDEEVVR LHLGSLDVHL TKLTQKQADY INVPVEGPYK
     SDAYRY