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 15-DEC-1998 (Rel. 37, Last annotation update) DE ADENOSYLHOMOCYSTEINASE (EC 3.3.1.1) (S-ADENOSYL-L-HOMOCYSTEINE DE HYDROLASE) (ADOHCYASE). GN AHCY. OS Rhodobacter capsulatus (Rhodopseudomonas capsulata). OC Bacteria; Proteobacteria; alpha subdivision; Rhodobacter group; OC Rhodobacter. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SB1003 / ST LOUIS; RX MEDLINE; 92335291. 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. 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 RT S-adenosyl-L-homocysteine hydrolase expression and is a member of the RT LysR family."; RL J. Bacteriol. 176:61-69(1994). CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-HOMOCYSTEINE + H(2)O = CC ADENOSINE + L-HOMOCYSTEINE. CC -!- COFACTOR: NAD. CC -!- PATHWAY: ACTIVATED METHYL CYCLE. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SIMILARITY: BELONGS TO THE ADENOSYLHOMOCYSTEINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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 INTERPRO; IPR000043; -. DR PFAM; PF00670; AdoHcyase; 1. DR PROSITE; PS00738; ADOHCYASE_1; 1. DR PROSITE; PS00739; ADOHCYASE_2; 1. KW Hydrolase; NAD; One-carbon metabolism. FT NP_BIND 247 278 NAD (POTENTIAL). 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 //