SAHH_PETCR
ID SAHH_PETCR Reviewed; 485 AA.
AC Q01781;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, 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;
GN Name=SAHH; Synonyms=SHH;
OS Petroselinum crispum (Parsley) (Petroselinum hortense).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Apieae; Petroselinum.
OX NCBI_TaxID=4043;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=1374911; DOI=10.1073/pnas.89.10.4713;
RA Kawalleck P., Plesch G., Hahlbrock K., Somssich I.E.;
RT "Induction by fungal elicitor of S-adenosyl-L-methionine synthetase and S-
RT adenosyl-L-homocysteine hydrolase mRNAs in cultured cells and leaves of
RT Petroselinum crispum.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4713-4717(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 259-485.
RA Somssich I.E., Bollmann J., Hahlbrock K., Kombrink E., Schulz W.;
RT "Differential early activation of defense-related genes in elicitor-treated
RT parsley cells.";
RL Plant Mol. Biol. 12:227-234(1989).
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.
CC -!- TISSUE SPECIFICITY: Mainly in floral buds and stems.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000305}.
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DR EMBL; M81885; AAA33856.1; -; mRNA.
DR EMBL; M62756; AAA33855.1; -; mRNA.
DR PIR; T15035; T15035.
DR AlphaFoldDB; Q01781; -.
DR SMR; Q01781; -.
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_0000116928"
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"
FT CONFLICT 346
FT /note="C -> D (in Ref. 1; AAA33855)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="L -> C (in Ref. 1; AAA33855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 53181 MW; 05E926516C2E08E6 CRC64;
MALSVEKTAA GREYKVKDMS LADFGRLELE LAEVEMPGLM SCRTEFGPSQ PFKGARITGS
LHMTIQTGVL IETLTALGAE VRWCSCNIFS TQDHAAAAIA RDSCAVFAWK GETLQEYWWC
TERALDWGPD GGPDLIVDDG GDATLLIHEG VKAEEEYKKS GAIPDPASTD NAEFQIVLSI
IRDGLKSDPM KYHKMKDRLV GVSEETTTGV KRLYQMQQNG TLLFPAINVN DSVTKSKFDN
LYGCRHSLPD GLMRATDVMI AGKVALIAGY GDVGKGCAAA MKQAGARVIV TEIDPICALQ
ATMEGLQVLP LEDVVSEVDI FVTTTGNKDI IMVSDMRKMK NNAIVCNIGH FDNEIDMLGL
ETYPGVKRIT IKPQTDRWVF PDTGRGIIIL AEGRLMNLGC ATGHPSFVMS CSFTNQVIAQ
LELWNEKSSG KYEKKVYVLP KHLDEKVAAL HLGKLGAKLT KLSKDQADYI SVPVEGPYKP
AHYRY
