ID   SAHHB_XENLA             Reviewed;         433 AA.
AC   O93477; Q6DKD5;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Adenosylhomocysteinase B;
DE            Short=AdoHcyase B;
DE            EC=3.3.1.1 {ECO:0000250|UniProtKB:P10760};
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase B;
GN   Name=ahcy-b; Synonyms=ahcy2, sahh;
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=Ovary;
RA   Radomski N., Plessmann U., Mohl C., Weber K., Dreyer C.;
RT   "S-adenosylhomocysteine hydrolase.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ007835; CAA07706.1; -; mRNA.
DR   EMBL; BC074224; AAH74224.1; -; mRNA.
DR   RefSeq; NP_001089040.1; NM_001095571.1.
DR   AlphaFoldDB; O93477; -.
DR   SMR; O93477; -.
DR   MaxQB; O93477; -.
DR   PRIDE; O93477; -.
DR   DNASU; 503682; -.
DR   GeneID; 503682; -.
DR   KEGG; xla:503682; -.
DR   CTD; 503682; -.
DR   Xenbase; XB-GENE-950023; ahcy.S.
DR   OMA; CLHVEAK; -.
DR   OrthoDB; 371693at2759; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 503682; Expressed in ovary and 20 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; -; 2.
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 B"
FT                   /id="PRO_0000116907"
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;  47745 MW;  3CB91D67C555B47C CRC64;
     MSDKLSYKVA DISLADWGRK AIEIAENEMP GLMKMREMYS ESKPLKGARI AGCLHMTLQT
     AVLIETLTAI GAEVQWSSCN IFSTQDHAAA AIAKTGVPVY AWKGETDEEY IWCIEQTIYF
     KDGKPLNMIL DDGGDLTNLV HTKYPQLLKG IKGISEETTT GVHNLYKMKS SGTLQVPAIN
     VNDSVTKSKF DNLYGCRESL IDGIKRATDV MIAGKVAVVA GYGDVGKGCA QALRAFGARV
     LITEIDPINA LQAAMEGYEV TTMDEASKEG NIFVTTTGCA DIVEGRHFEN MKDDSIVCNI
     GHFDVELDVK WLNDNAAKKI NIKPQVDRYL LKNGRHIILL AEGRLVNLGC AMGHPSFVMS
     NSFTNQVMAQ IELWTNTDKY PVGVYFLPKK LDEAVAAAHL DKLGVKLTKL TDKQAKYLGL
     DKEGPFKPDH YRY