ID   SAHHA_XENLA             Reviewed;         433 AA.
AC   P51893; Q6GNV1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Adenosylhomocysteinase A;
DE            Short=AdoHcyase A;
DE            EC=3.3.1.1 {ECO:0000250|UniProtKB:P10760};
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase A;
GN   Name=ahcy-a; Synonyms=ahcy, ahcy1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7811234; DOI=10.1006/bbrc.1994.2842;
RA   Seery L.T., McCabe B.D., Schoenberg D.R., Whitehead A.S.;
RT   "S-adenosyl-L-homocysteine hydrolase from Xenopus laevis -- identification,
RT   developmental expression and evolution.";
RL   Biochem. Biophys. Res. Commun. 205:1539-1546(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of S-adenosyl-L-homocysteine to form
CC       adenosine and homocysteine (By similarity). Binds copper ions (By
CC       similarity). {ECO:0000250|UniProtKB:P10760,
CC       ECO:0000250|UniProtKB:P50247}.
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         Evidence={ECO:0000250|UniProtKB:P10760};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21709;
CC         Evidence={ECO:0000250|UniProtKB:P10760};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000250|UniProtKB:P10760};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000250|UniProtKB:P10760};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P10760}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23526}.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000305}.
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DR   EMBL; L35559; AAA65963.1; -; mRNA.
DR   EMBL; BC060432; AAH60432.1; -; mRNA.
DR   EMBL; BC073400; AAH73400.1; -; mRNA.
DR   PIR; JC2480; JC2480.
DR   RefSeq; NP_001089027.1; NM_001095558.1.
DR   AlphaFoldDB; P51893; -.
DR   SMR; P51893; -.
DR   DNASU; 503669; -.
DR   GeneID; 503669; -.
DR   KEGG; xla:503669; -.
DR   CTD; 503669; -.
DR   Xenbase; XB-GENE-6251978; ahcy.L.
DR   OMA; NKYGCRE; -.
DR   OrthoDB; 371693at2759; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 503669; Expressed in pancreas and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; ISS:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
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; 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   Copper; Cytoplasm; Hydrolase; NAD; One-carbon metabolism;
KW   Reference proteome.
FT   CHAIN           1..433
FT                   /note="Adenosylhomocysteinase A"
FT                   /id="PRO_0000116906"
FT   REGION          184..351
FT                   /note="NAD binding"
FT                   /evidence="ECO:0000250|UniProtKB:P10760"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10760"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10760"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10760"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10760"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10760"
SQ   SEQUENCE   433 AA;  47747 MW;  28C7DB273199F2FA CRC64;
     MSDKLSYKVA DISLADWGRK AIEIAENEMP GLMKMREMHS ESKPLKGARI AGCLHMTLQT
     AVLIETLTAL GAEVQWSSCN IFSTQDHAAA AIAKTGVPVY AWKGETDEEY IWCIEQTIYF
     KDGKPLNMIL DDGGDLTNLV HSKYPQLLKG IKGISEETTT GVHNLYKMKS SGTLQVPAIN
     VNDSVTKSKF DNLYGCRESL IDGIKRATDV MIAGKVAVVA GYGDVGKGCA QALRAFGARV
     IITEIDPINA LQAAMEGYEV TTMDEASKEG NIFVTTTGCA DIVEGRHFEN MKDDSIVCNI
     GHFDIELDVK WLNENAVKKV NIKPQVDRYL LKNGRHIILL AEGRLVNLGC AMGHPSFVMS
     NSFTNQVMAQ IELWTNTDKY PVGVYFLPKK LDEAVAAAHL DKLGVKLTKL TDKQAKYLGL
     DKEGPFKPDH YRY