ID SAHH_BURP6 Reviewed; 473 AA. AC A3NER1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 04-NOV-2026, entry version 106. 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=BURPS668_3838; OS Burkholderia pseudomallei (strain 668). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320373; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=668; RX PubMed=20333227; DOI=10.1093/gbe/evq003; RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S., RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J., RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P., RA Nierman W.C.; RT "Continuing evolution of Burkholderia mallei through genome reduction and RT large-scale rearrangements."; RL Genome Biol. Evol. 2:102-116(2010). 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; CP000570; ABN83154.1; -; Genomic_DNA. DR RefSeq; WP_004198634.1; NC_009074.1. DR SMR; A3NER1; -. DR GeneID; 93061911; -. DR KEGG; bpd:BURPS668_3838; -. DR HOGENOM; CLU_025194_2_1_4; -. DR OMA; AACIKGV; -. DR UniPathway; UPA00314; UER00076. DR CDD; cd00401; SAHH; 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 AlphaFoldDB; A3NER1; -. PE 3: Inferred from homology; KW Cytoplasm; Hydrolase; NAD; One-carbon metabolism. FT CHAIN 1..473 FT /note="Adenosylhomocysteinase" FT /id="PRO_1000024719" FT BINDING 64 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 139 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 199 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 200..202 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 229 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 233 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 234 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 263..268 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 286 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 321 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 342..344 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 387 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" SQ SEQUENCE 473 AA; 52201 MW; 7A40ECDD0A47B596 CRC64; MNAAVIDSHS AQDYVVADIA LAGWGRKELN IAETEMPGLV QIRDEYKAQQ PLKGARIAGS LHMTIQTGVL IETLKALGAD VRWASCNIFS TQDHAAAAIV EAGTPVFAFK GESLDEYWEF SHRIFEWPNG EFANMILDDG GDATLLLILG SKAEKDRSVI ARPTNEEEVA LFKSIERHLE IDGSWYSKRL AHIKGVTEET TTGVHRLYQM EKDGRLPFPA FNVNDSVTKS KFDNLYGCRE SLVDGIKRAT DVMIAGKIAV VAGYGDVGKG CAQSLRGLGA TVWVTEIDPI CALQAAMEGY RVVTMEYAAD KADIFVTATG NYHVINHDHM KAMRHNAIVC NIGHFDSEID VASTRQYQWE NIKPQVDHII FPDGKRVILL AEGRLVNLGC ATGHPSFVMS NSFTNQTLAQ IELFTRGGEY ANKVYVLPKH LDEKVARLHL ARIGAQLSEL SDDQAAYIGV SKAGPFKPDH YRY //