ID SAHH_HALS3 Reviewed; 427 AA. AC B0R7F2; DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 02-SEP-2026, entry version 99. DE RecName: Full=Adenosylhomocysteinase {ECO:0000255|HAMAP-Rule:MF_00563}; DE EC=3.13.2.1 {ECO:0000255|HAMAP-Rule:MF_00563}; DE AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000255|HAMAP-Rule:MF_00563}; DE Short=AdoHcyase {ECO:0000255|HAMAP-Rule:MF_00563}; GN Name=ahcY {ECO:0000255|HAMAP-Rule:MF_00563}; GN OrderedLocusNames=OE_4159F; OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Halobacteria; Halobacteriales; Halobacteriaceae; Halobacterium; OC Halobacterium salinarum NRC-34001. OX NCBI_TaxID=478009; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29341 / DSM 671 / R1; RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001; RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K., RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.; RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain RT R1 compared to that of strain NRC-1."; RL Genomics 91:335-346(2008). CC -!- FUNCTION: May play a key role in the regulation of the intracellular CC concentration of adenosylhomocysteine. {ECO:0000255|HAMAP- CC Rule:MF_00563}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine; 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:0000255|HAMAP-Rule:MF_00563}; CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00563}; CC Note=Binds 1 NAD(+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00563}; CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L- CC homocysteine from S-adenosyl-L-homocysteine: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00563}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00563}. CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family. CC {ECO:0000255|HAMAP-Rule:MF_00563, 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; AM774415; CAP14671.1; -; Genomic_DNA. DR RefSeq; WP_010903672.1; NC_010364.1. DR AlphaFoldDB; B0R7F2; -. DR SMR; B0R7F2; -. DR EnsemblBacteria; CAP14671; CAP14671; OE_4159F. DR GeneID; 68694802; -. DR KEGG; hsl:OE_4159F; -. DR HOGENOM; CLU_025194_0_2_2; -. DR PhylomeDB; B0R7F2; -. DR UniPathway; UPA00314; UER00076. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0071269; P:L-homocysteine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0033353; P:L-methionine cycle; IEA:TreeGrafter. DR CDD; cd00401; SAHH; 1. DR Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR00936; ahcY; 1. DR NCBIfam; NF004005; PRK05476.2-3; 1. DR PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1. DR PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 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; 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 Cytoplasm; Hydrolase; NAD; One-carbon metabolism. FT CHAIN 1..427 FT /note="Adenosylhomocysteinase" FT /id="PRO_0000416094" FT BINDING 132 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 157 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 158..160 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 187 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 191 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 192 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 221..226 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 244 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 279 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 300..302 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 347 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" SQ SEQUENCE 427 AA; 45907 MW; 6131D032241E1377 CRC64; MTTAPAISSR LDDPESARET GRAKIDWAFE HMPILSALRE EFDANQPLAG ETIGMAMHVE AKTAALVETM ADAGAEIAIT GCNPLSTHDG VSAALDAHES ITSYAERGAE GEAYYDAIDA VLAHEPTVTV DDGGDLVFRV HEDHPELIDT IIGGTEETTT GVHRLRAMDD DDALEYPVFA VNDTPMKRLF DNVHGTGESA LANIAMTTNL SWAGKDVVVA GYGDCGRGVA KKAAGQNANV IVTEVEPRRA LEAHMEGYDV MPMAEAAEVG DVFLTTTGNK NVITRAHFER MDDGVVLANA GHFDVEVNLD HLSELAVSER EAREGVREYE LADGRRLNVL AEGRLVNLAS PIGLGHPVGV MDQSFGVQAV CVRELVANRE EYAAGVHNVP DELDIEIAEI KLAAEGVEYD ALTDDQAEYM DSWQHGT //