ID D5AKH2_RHOCB Unreviewed; 463 AA. AC D5AKH2; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 31-MAY-2011, entry version 9. DE RecName: Full=Adenosylhomocysteinase; DE EC=3.3.1.1; DE AltName: Full=S-adenosyl-L-homocysteine hydrolase; GN Name=ahcY; OrderedLocusNames=RCAP_rcc00049; OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=272942; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SB1003; RA Strnad H., Lapidus A., Vlcek C., Ulbrich P., Paces J., Maltsev N., RA Kumar V., Kogan Y., Milgram A., Rebrekov D., Mazur M., Cox R., RA Kyrpides N., Kolar M., Sachova J., Ridl J., Ivanova N., Kapatral V., RA Los T., Lykidis A., Mikhailova N., Reznik G., Vasieva O., Fonstein M., RA Paces V., Haselkorn R.; RT "Complete genome sequence of Rhodobacter capsulatus SB1003."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20418398; DOI=10.1128/JB.00366-10; RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., RA Haselkorn R.; RT "Complete genome sequence of the photosynthetic purple nonsulfur RT bacterium Rhodobacter capsulatus SB 1003."; RL J. Bacteriol. 192:3545-3546(2010). 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 (By similarity). CC -!- COFACTOR: NAD (By similarity). CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L- CC homocysteine from S-adenosyl-L-homocysteine: step 1/1. 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 https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001312; ADE83814.1; -; Genomic_DNA. DR RefSeq; YP_003576221.1; NC_014034.1. DR GeneID; 9002878; -. DR GenomeReviews; CP001312_GR; RCAP_rcc00049. DR KEGG; rcp:RCAP_rcc00049; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:HAMAP. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:HAMAP. 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 Complete proteome; Cytoplasm; Hydrolase; NAD; One-carbon metabolism. 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; 50594 MW; 44EBA9744B2FCA24 CRC64; MADYIVKDIK LAEFGRKELD IAETEMPGLM ACREEFGPSQ PLKGARIAGS LHMTIQTAVL IETLKALGAD VRWASCNIFS TQDHAAAAIA AGGTPVFAVK GETLEEYWAY TDKIFQFPEG TCNMILDDGG DATLYILLGA RVEAGETDLI ATPTSEEEVC 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 //