ID SAHH_HAHCH Reviewed; 463 AA. AC Q2SLT4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 16-JUN-2009, entry version 29. 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=HCH_01532; OS Hahella chejuensis (strain KCTC 2396). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Hahellaceae; Hahella. OX NCBI_TaxID=349521; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16352867; DOI=10.1093/nar/gki1016; RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., RA Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., RA Park H.-S., Lee H.K., Oh T.K., Kim J.F.; RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing RT an algicidal agent."; RL Nucleic Acids Res. 33:7066-7073(2005). 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; CP000155; ABC28390.1; -; Genomic_DNA. DR RefSeq; YP_432815.1; -. DR GeneID; 3837562; -. DR GenomeReviews; CP000155_GR; HCH_01532. DR KEGG; hch:HCH_01532; -. DR NMPDR; fig|349521.5.peg.1378; -. DR HOGENOM; Q2SLT4; -. DR OMA; Q2SLT4; HMRAMKD. DR BioCyc; HCHE349521:HCH_01532-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 1 463 Adenosylhomocysteinase. FT /FTId=PRO_1000024728. FT REGION 191 373 NAD binding (By similarity). FT BINDING 63 63 Substrate (By similarity). FT BINDING 139 139 Substrate (By similarity). FT BINDING 164 164 Substrate (By similarity). FT BINDING 194 194 Substrate (By similarity). FT BINDING 198 198 Substrate (By similarity). SQ SEQUENCE 463 AA; 51348 MW; 40D703C8EAE28FF6 CRC64; MAQLQSVDNF SDYKVKDISL AAWGRKEIDI AEGEMPALMT LREKYRAQQP LAGARILGCI HMTIQTAVLI ETLVALGAEV RWSSCNIFST QDHAAAAIAA AGVPVFAWKG ETEEEYVWCI KQTITKDGQP WNANMVLDDG GDLTEILHNE FPQMLDHIHG ISEETTTGVH RLLDMMKKGE LKVPAVNVND SVTKSKNDNK YGCRHSLNDA IKRATDHLLA GKKALVIGYG DVGKGSAASL RQEGMIVKIS EIDPICAMQA CMDGYEVVSP YIDGVNTGAA DGVNRDLLGH TDLLVTTTGN VNVCDKYMLQ ALKSGAVVCN IGHFDNEIDT RFMRDNWEWE EVKPQVHVIY RNKDQNDHLL LLSEGRLVNL GNATGHPSRI MDGSFANQVL AQMYLFERKF ADLPADEKPK NLYVRVLPKQ LDEEVARYMV QGFGGVITKL TQPQAKYIGV EVEGPYKPTD YKY //