ID SAHH_HALHL Reviewed; 430 AA. AC A1WXM7; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 04-NOV-2026, entry version 107. 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=Hhal_1675; OS Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira OS halophila (strain DSM 244 / SL1)). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Chromatiales; Ectothiorhodospiraceae; Halorhodospira. OX NCBI_TaxID=349124; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 244 / SL1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W., RA Richardson P.; RT "Complete sequence of Halorhodospira halophila SL1."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. 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}. 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; CP000544; ABM62439.1; -; Genomic_DNA. DR RefSeq; WP_011814461.1; NC_008789.1. DR SMR; A1WXM7; -. DR STRING; 349124.Hhal_1675; -. DR KEGG; hha:Hhal_1675; -. DR eggNOG; COG0499; Bacteria. DR HOGENOM; CLU_025194_2_1_6; -. DR OMA; AACIKGV; -. DR OrthoDB; 9802717at2; -. DR UniPathway; UPA00314; UER00076. DR CDD; cd00401; SAHH; 1. DR FunFam; 3.40.50.1480:FF:000004; Adenosylhomocysteinase; 1. DR FunFam; 3.40.50.720:FF:000004; Adenosylhomocysteinase; 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 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 NCBIfam; TIGR00936; ahcY; 1. DR NCBIfam; NF004005; PRK05476.2-3; 1. DR PROSITE; PS00738; ADOHCYASE_1; 1. DR PROSITE; PS00739; ADOHCYASE_2; 1. 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 Proteomes; UP000000647; Chromosome. DR AlphaFoldDB; A1WXM7; -. PE 3: Inferred from homology; KW Cytoplasm; Hydrolase; NAD; One-carbon metabolism; Reference proteome. FT CHAIN 1..430 FT /note="Adenosylhomocysteinase" FT /id="PRO_1000061125" FT BINDING 56 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 131 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 156 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 157..159 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 186 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 190 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 191 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 220..225 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 243 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 278 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 299..301 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 344 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" SQ SEQUENCE 430 AA; 47510 MW; 1B0D75461642D506 CRC64; MSNQDYKVAD ISLADWGRKE IKIAESEMPG LMETRREFAA QKPLKGARIA GCLHMTIQTA VLIETLQELG AEVRWSSCNI FSTQDQAAAA VAANGTPVFA WKGETEEEYW WCIEQTINGP DGWKPNMLLD DGGDLTAVIH EQYPDMMKDI YGVSEETTTG VHRLYEMSRK GELGMPAFNV NDSVTKSKFD NLYGCRESLV DSIKRATDVM IAGKVAVVAG FGDVGKGSAQ SLRGLGAQVW VTEVDPICAL QASMDGYKVV TMEEAAPVAD IFVTATGNYN VITHDHMKAM KDEAIVCNIG HFDNEIDVAS LKQYKWDEIK PQVDHVEFPD GKKITLLAEG RLVNLGCATG HPSFVMSNSF TNQVMAQMEL YNNPGKYEKD VYVLPKHLDE KVAALHLGRV GANLTRLSEE QAGYIGVSVD GPFKPEWYRY //