ID SAHH_RHOCA STANDARD; PRT; 463 AA. AC P28183; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Adenosylhomocysteinase (EC 3.3.1.1) (S-adenosyl-L-homocysteine DE hydrolase) (AdoHcyase). GN Name=ahcY; OS Rhodobacter capsulatus (Rhodopseudomonas capsulata). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=1061; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SB1003 / St Louis; RX MEDLINE=92335291; PubMed=1631127; RA Sganga M.W., Aksamit R.R., Cantoni G.L., Bauer C.E.; RT "Mutational and nucleotide sequence analysis of S-adenosyl-L- RT homocysteine hydrolase from Rhodobacter capsulatus."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6328-6332(1992). RN [2] RP SEQUENCE OF 1-13 FROM N.A. RC STRAIN=SB1003 / St Louis; RX MEDLINE=94110241; PubMed=8282711; RA Buggy J.J., Sganga M.W., Bauer C.E.; RT "Nucleotide sequence and characterization of the Rhodobacter RT capsulatus hvrB gene: HvrB is an activator of S-adenosyl-L- RT homocysteine hydrolase expression and is a member of the LysR RT family."; RL J. Bacteriol. 176:61-69(1994). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = L- CC homocysteine + adenosine. CC -!- COFACTOR: Binds 1 NAD per subunit. CC -!- PATHWAY: Activated methyl cycle. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity). CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family. 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; M80630; AAA26094.1; -. DR EMBL; L23836; AAA53540.1; -. DR PIR; A46035; A46035. DR HSSP; P10760; 1B3R. DR HAMAP; MF_00563; -; 1. DR InterPro; IPR000043; Ad_hcy_hydrolase. DR Pfam; PF05221; AdoHcyase; 1. DR Pfam; PF00670; AdoHcyase_NAD; 1. DR TIGRFAMs; TIGR00936; ahcY; 1. DR PROSITE; PS00738; ADOHCYASE_1; 1. DR PROSITE; PS00739; ADOHCYASE_2; 1. KW Hydrolase; NAD; One-carbon metabolism. FT DOMAIN 216 381 NAD binding (By similarity). FT BINDING 54 54 Substrate (By similarity). FT BINDING 128 128 Substrate (By similarity). FT BINDING 189 189 Substrate (By similarity). FT BINDING 219 219 Substrate (By similarity). FT BINDING 223 223 Substrate (By similarity). SQ SEQUENCE 463 AA; 50580 MW; E4EB19B320420B53 CRC64; MADYIVKDIK LAEFGRKELD IAETEMPGLM ACREEFGPSQ PLKGARIAGS LHMTIQTAVL IETLKALGAD VRWASCNIFS TQDHAAAAIA AGGTPVFAVK GETLEEYWAY TDKIFQFPEG TCNMILDDGG DATLYILLGA RVEAGETDLI ATPTSEDEVC LFNQIKKRMV ESPGWFTQQR AAIKGVSEET TTGVHRLYDL HKKGLLPFPA INVNDSVTKS KFDNKYGCKE SLVDGIRRAT DVMMAGKVAV VCGYGDVGKG SAASLRGAGA RVKVTEVDPI CALQAAMDGF EVVVLEDVVA DADIFITTTG NKDVIRIEHM REMKDMAIVG NIGHFDNEIQ VAALKNHKWT NIKDQVDMIE MPSGARIILL SEGRLLNLGN ATGHPSFVMS ASFTNQVLAQ IELWTKGAEY QPGVYILPKS LDEKVARLHL KKIGVKLTTL RPDQAEYIGV TVEGPFKSDH YRY //