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Database: UniProt
Entry: A0A2G2ZTN5_CAPAN
LinkDB: A0A2G2ZTN5_CAPAN
Original site: A0A2G2ZTN5_CAPAN 
ID   A0A2G2ZTN5_CAPAN        Unreviewed;       343 AA.
AC   A0A2G2ZTN5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Adenosylhomocysteinase {ECO:0000256|ARBA:ARBA00022091};
DE            EC=3.13.2.1 {ECO:0000256|ARBA:ARBA00034527};
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000256|ARBA:ARBA00033091};
GN   ORFNames=T459_07429 {ECO:0000313|EMBL:PHT85323.1};
OS   Capsicum annuum (Capsicum pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=4072 {ECO:0000313|EMBL:PHT85323.1, ECO:0000313|Proteomes:UP000222542};
RN   [1] {ECO:0000313|EMBL:PHT85323.1, ECO:0000313|Proteomes:UP000222542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. CM334 {ECO:0000313|Proteomes:UP000222542};
RX   PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA   Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA   Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA   Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA   Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA   Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA   Bennetzen J.L., Choi D.;
RT   "New reference genome sequences of hot pepper reveal the massive evolution
RT   of plant disease-resistance genes by retroduplication.";
RL   Genome Biol. 18:R210.1-R210.11(2017).
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:0000256|ARBA:ARBA00002639}.
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=3.13.2.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00034436};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005195}.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000256|ARBA:ARBA00007122}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PHT85323.1}.
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DR   EMBL; AYRZ02000003; PHT85323.1; -; Genomic_DNA.
DR   STRING; 4072.A0A2G2ZTN5; -.
DR   EnsemblPlants; PHT85323; PHT85323; T459_07429.
DR   Gramene; PHT85323; PHT85323; T459_07429.
DR   OMA; NIACADG; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000222542; Chromosome 3.
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   Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; ADENOSYLHOMOCYSTEINASE; 1.
DR   PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
DR   Pfam; PF00670; AdoHcyase_NAD; 1.
DR   SMART; SM00996; AdoHcyase; 1.
DR   SMART; SM00997; AdoHcyase_NAD; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00738; ADOHCYASE_1; 1.
DR   PROSITE; PS00739; ADOHCYASE_2; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000222542}.
FT   DOMAIN          240..343
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
SQ   SEQUENCE   343 AA;  37095 MW;  C1117A7AD4D86103 CRC64;
     MALLVEKTNS GREYKVKDMS QADFGRLKIE LAEVEMPGLM ACRTEFGPSQ PFKGAKITGS
     LHMTIQTAVL IETLTALGAE VRWCSCNIFS TQDHAAAAIA RDSAAVFAWK GETLQEYWWC
     TERALDWGPG GGPDLIVDDG GDATLLIHEG VKAEEEFAKN GTVPDPSSTD NVEFQLVLGI
     IKESLKVDPL RYTKMKERLV GVSEETTTGV KRLYQMQANG TLLFPAINVN DSVTKSKFDN
     LYGCRHSLPD GLMRATDVMI AGKVAFIAGY GDVGKGCAAA MKQAGARVIV SEIDPICALQ
     ATMEGLQVLP LEDVVSDVDI FVTTTXISLS PPPVTRTSSW LTI
//
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