ID SAHH_MESSB Reviewed; 465 AA. AC Q11CD0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 16-JUN-2009, entry version 27. DE RecName: Full=Adenosylhomocysteinase; DE EC=3.3.1.1; DE AltName: Full=S-adenosyl-L-homocysteine hydrolase; DE Short=AdoHcyase; GN Name=ahcY; OrderedLocusNames=Meso_3576; OS Mesorhizobium sp. (strain BNC1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=266779; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Richardson P.; RT "Complete sequence of chromosome of Mesorhizobium sp. BNC1."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = L- CC homocysteine + adenosine. CC -!- COFACTOR: Binds 1 NAD per subunit (By similarity). CC -!- PATHWAY: Amino-acid biosynthesis; homocysteine biosynthesis; L- CC homocysteine from S-adenosyl-L-homocysteine: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000390; ABG64945.1; -; Genomic_DNA. DR RefSeq; YP_676110.1; -. DR GeneID; 4181405; -. DR GenomeReviews; CP000390_GR; Meso_3576. DR KEGG; mes:Meso_3576; -. DR NMPDR; fig|266779.1.peg.960; -. DR HOGENOM; Q11CD0; -. DR OMA; Q11CD0; HMRAMKD. DR BioCyc; MSP266779:MESO_3576-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:HAMAP. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0006730; P:one-carbon compound metabolic process; IEA:HAMAP. DR HAMAP; MF_00563; -; 1. DR InterPro; IPR000043; Ad_hcy_hydrolase. DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd. DR Gene3D; G3DSA:3.40.50.1480; Ad_hcy_hydrolase; 1. DR PANTHER; PTHR23420; Ad_hcy_hydrolase; 1. DR Pfam; PF05221; AdoHcyase; 1. DR Pfam; PF00670; AdoHcyase_NAD; 1. DR PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1. DR TIGRFAMs; TIGR00936; ahcY; 1. DR PROSITE; PS00738; ADOHCYASE_1; 1. DR PROSITE; PS00739; ADOHCYASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; NAD; One-carbon metabolism. FT CHAIN 1 465 Adenosylhomocysteinase. FT /FTId=PRO_1000024731. FT REGION 218 383 NAD binding (By similarity). FT BINDING 56 56 Substrate (By similarity). FT BINDING 131 131 Substrate (By similarity). FT BINDING 191 191 Substrate (By similarity). FT BINDING 221 221 Substrate (By similarity). FT BINDING 225 225 Substrate (By similarity). SQ SEQUENCE 465 AA; 50894 MW; 2D5217D543BE535F CRC64; MAADDYVVAD MSLAAWGRKE IEIAETEMPG LMACREEFGE AKPLKGARIT GSLHMTIQTA VLIETLKSLG AEVRWASCNI FSTQDHAAAA IAETGTPVFA VKGETLEEYW TYTDRIFQWP DGQPSNMILD DGGDATMYIL LGARAEAGED VLSNPDGEEE EILFQQIKKR MAETPGFFTR QRAAIRGVTE ETTTGVNRLY QLQKKGLLPF PAINVNDSVT KSKFDNKYGC KESLVDGIRR ATDVMMAGKV AIVCGYGDVG KGSAQSLAGA GARVKVTEAD PICALQAAMD GFEVVTLDEA IATADIIITA TGNKDVVSLD HMRKMKDMVI LGNIGHFDNE IQVAALRNFK WVNIKPQVDL IEFPDGKRII LLSEGRLLNL GNATGHPSFV MSASFTNQVL AQIELWTRGS QYENKVYVLP KHLDEKVARL HLAKLGANLT KLSPEQAAYI GVTPEGPFKP DHYRY //