ID SAHH_RHOCA Reviewed; 463 AA. AC P28183; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 05-OCT-2010, entry version 69. DE RecName: Full=Adenosylhomocysteinase; DE EC=3.3.1.1; DE AltName: Full=S-adenosyl-L-homocysteine hydrolase; DE Short=AdoHcyase; GN Name=ahcY; OS Rhodobacter capsulatus (Rhodopseudomonas capsulata). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=1061; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 23782 / LMG 2373 / NCIB 11773 / SB1003 / St. Louis; RX MEDLINE=92335291; PubMed=1631127; DOI=10.1073/pnas.89.14.6328; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13. RC STRAIN=ATCC 23782 / LMG 2373 / NCIB 11773 / 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 -!- FUNCTION: May play a key role in the regulation of the CC intracellular concentration of adenosylhomocysteine (By CC similarity). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = L- CC homocysteine + adenosine. CC -!- COFACTOR: Binds 1 NAD per subunit. CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L- CC homocysteine from S-adenosyl-L-homocysteine: step 1/1. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm (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; -; Genomic_DNA. DR EMBL; L23836; AAA53540.1; -; Genomic_DNA. DR PIR; A46035; A46035. DR ProteinModelPortal; P28183; -. DR SMR; P28183; 3-463. DR BRENDA; 3.3.1.1; 567. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:EC. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. DR HAMAP; MF_00563; AdoHcyase; 1; -. DR InterPro; IPR000043; Adenosylhomocysteinase. DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd. DR InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS. 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 Cytoplasm; Hydrolase; NAD; One-carbon metabolism. FT CHAIN 1 463 Adenosylhomocysteinase. FT /FTId=PRO_0000116983. FT NP_BIND 190 192 NAD (By similarity). FT NP_BIND 253 258 NAD (By similarity). FT NP_BIND 332 334 NAD (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). FT BINDING 224 224 NAD (By similarity). FT BINDING 276 276 NAD (By similarity). FT BINDING 311 311 NAD (By similarity). FT BINDING 377 377 NAD (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 //