ID SAHH_RHOCB Reviewed; 463 AA. AC P28183; D5AKH2; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 2. DT 03-MAY-2023, entry version 128. DE RecName: Full=Adenosylhomocysteinase {ECO:0000255|HAMAP-Rule:MF_00563}; DE EC=3.13.2.1 {ECO:0000255|HAMAP-Rule:MF_00563}; DE AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000255|HAMAP-Rule:MF_00563}; DE Short=AdoHcyase {ECO:0000255|HAMAP-Rule:MF_00563}; GN Name=ahcY {ECO:0000255|HAMAP-Rule:MF_00563}; GN OrderedLocusNames=RCAP_rcc00049; OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Rhodobacter. OX NCBI_TaxID=272942; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003; RX 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-homocysteine RT hydrolase from Rhodobacter capsulatus."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6328-6332(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003; 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 bacterium RT Rhodobacter capsulatus SB 1003."; RL J. Bacteriol. 192:3545-3546(2010). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003; RX PubMed=8282711; DOI=10.1128/jb.176.1.61-69.1994; RA Buggy J.J., Sganga M.W., Bauer C.E.; RT "Nucleotide sequence and characterization of the Rhodobacter capsulatus RT hvrB gene: HvrB is an activator of S-adenosyl-L-homocysteine hydrolase RT expression and is a member of the LysR family."; RL J. Bacteriol. 176:61-69(1994). CC -!- FUNCTION: May play a key role in the regulation of the intracellular CC concentration of adenosylhomocysteine. {ECO:0000255|HAMAP- CC Rule:MF_00563}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine; CC Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00563}; CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Note=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 {ECO:0000255|HAMAP-Rule:MF_00563}. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00563}. CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family. CC {ECO:0000255|HAMAP-Rule:MF_00563}. 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; CP001312; ADE83814.1; -; Genomic_DNA. DR EMBL; L23836; AAA53540.1; -; Genomic_DNA. DR PIR; A46035; A46035. DR RefSeq; WP_013065796.1; NC_014034.1. DR AlphaFoldDB; P28183; -. DR SMR; P28183; -. DR STRING; 272942.RCAP_rcc00049; -. DR EnsemblBacteria; ADE83814; ADE83814; RCAP_rcc00049. DR GeneID; 31489006; -. DR KEGG; rcp:RCAP_rcc00049; -. DR eggNOG; COG0499; Bacteria. DR HOGENOM; CLU_025194_2_1_5; -. DR OMA; YIGVTVE; -. DR OrthoDB; 9802717at2; -. DR UniPathway; UPA00314; UER00076. DR Proteomes; UP000002361; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd00401; SAHH; 1. DR Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00563; AdoHcyase; 1. DR InterPro; IPR042172; Adenosylhomocyst_ase-like_sf. DR InterPro; IPR000043; Adenosylhomocysteinase-like. DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS. DR PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1. DR PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 1. DR Pfam; PF05221; AdoHcyase; 1. DR Pfam; PF00670; AdoHcyase_NAD; 1. DR PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1. DR SMART; SM00996; AdoHcyase; 1. DR SMART; SM00997; AdoHcyase_NAD; 1. DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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; Reference proteome. FT CHAIN 1..463 FT /note="Adenosylhomocysteinase" FT /id="PRO_0000116983" FT BINDING 54 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 128 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 189 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 190..192 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 219 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 223 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 224 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 253..258 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 276 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 311 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 332..334 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT BINDING 377 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563" FT CONFLICT 157 FT /note="E -> D (in Ref. 1; AAA26094)" FT /evidence="ECO:0000305" 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 //