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SAHH_TOBAC
ID   SAHH_TOBAC              Reviewed;         485 AA.
AC   P68173; P50248;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Adenosylhomocysteinase;
DE            Short=AdoHcyase;
DE            EC=3.3.1.1;
DE   AltName: Full=Cytokinin-binding protein CBP57;
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase;
GN   Name=SAHH;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Bright Yellow 4;
RA   Tanaka H., Masuta C., Kataoka J., Kuwata S., Koiwai A., Noma M.;
RT   "Inducible expression by plant hormones of S-adenosyl-homocysteine
RT   hydrolase gene from Nicotiana tabacum during early flower bud formation in
RT   vitro.";
RL   Plant Sci. 113:167-174(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. {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   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000305}.
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DR   EMBL; D45204; BAA08142.1; -; mRNA.
DR   EMBL; D49804; BAA23164.1; -; Genomic_DNA.
DR   RefSeq; NP_001312346.1; NM_001325417.1.
DR   AlphaFoldDB; P68173; -.
DR   SMR; P68173; -.
DR   STRING; 4097.P68173; -.
DR   GeneID; 107786358; -.
DR   KEGG; nta:107786358; -.
DR   OMA; APIGDIF; -.
DR   PhylomeDB; P68173; -.
DR   BRENDA; 3.3.1.1; 3645.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IBA:GO_Central.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..485
FT                   /note="Adenosylhomocysteinase"
FT                   /id="PRO_0000116932"
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;  53104 MW;  AA6D6844E9DF0A5C CRC64;
     MALLVEKTTS GREYKVKDMS QADFGRLEIE LAEVEMPGLM ACRTEFGPSQ PFKGAKITGS
     LHMTIQTAVL IETLTALGAE VRWCSCNIFS TQDHAAAAIA RDSAAVFAWK GETLQEYWWC
     TERALDWGPG GGPDLIVDDG GDATLLIHEG VKAEEEFAKN GTIPDPNSTD NAEFQLVLTI
     IKESLKTDPL KYTKMKERLV GVSEETTTGV KRLYQMQANG TLLFPAINVN DSVTKSKFDN
     LYGCRHSLPD GLMRATDVMI AGKVALVAGY GDVGKGCAAA LKQAGARVIV TEIDPICALQ
     ATMEGLQVLT LEDVVSDVDI FVTTTGNKDI IMVDHMRKMK NNAIVCNIGH FDNEIDMLGL
     ETYPGVKRIT IKPQTDRWVF PDTNSGIIVL AEGRLMNLGC ATGHPSFVMS CSFTNQVIAQ
     LELWNEKSSG KYEKKVYVLP KHLDEKVAAL HLGKLGAKLT KLSKDQADYI SVPVEGPYKP
     AHYRY
 
 
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