ID SAHH_HYPNA Reviewed; 469 AA. AC Q0C427; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 27. DE RecName: Full=Adenosylhomocysteinase; DE EC=3.3.1.1; DE AltName: Full=S-adenosyl-L-homocysteine hydrolase; DE Short=AdoHcyase; GN Name=ahcY; OrderedLocusNames=HNE_0788; OS Hyphomonas neptunium (strain ATCC 15444). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Hyphomonas. OX NCBI_TaxID=228405; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16980487; DOI=10.1128/JB.00111-06; RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., RA Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., RA Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A., RA Rosovitz M.J., Madupu R., Brinkac L.M., Durkin A.S., Daugherty S.C., RA Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D., RA Davidsen T.M., Yang Q., Zafar N., Ward N.L.; RT "Comparative genomic evidence for a close relationship between the RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter RT crescentus."; RL J. Bacteriol. 188:6841-6850(2006). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = L- CC homocysteine + adenosine. CC -!- COFACTOR: Binds 1 NAD per subunit (By similarity). 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 http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000158; ABI76706.1; -; Genomic_DNA. DR RefSeq; YP_759516.1; -. DR GeneID; 4289748; -. DR GenomeReviews; CP000158_GR; HNE_0788. DR KEGG; hne:HNE_0788; -. DR NMPDR; fig|228405.5.peg.770; -. DR TIGR; HNE_0788; -. DR HOGENOM; Q0C427; -. DR OMA; Q0C427; HMRAMKD. DR BioCyc; HNEP81032:HNE_0788-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:HAMAP. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0006730; P:one-carbon compound metabolic process; IEA:HAMAP. DR HAMAP; MF_00563; -; 1. DR InterPro; IPR000043; Ad_hcy_hydrolase. DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd. DR Gene3D; G3DSA:3.40.50.1480; Ad_hcy_hydrolase; 1. 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 CHAIN 1 469 Adenosylhomocysteinase. FT /FTId=PRO_1000061126. FT REGION 222 387 NAD binding (By similarity). FT BINDING 60 60 Substrate (By similarity). FT BINDING 135 135 Substrate (By similarity). FT BINDING 195 195 Substrate (By similarity). FT BINDING 225 225 Substrate (By similarity). FT BINDING 229 229 Substrate (By similarity). SQ SEQUENCE 469 AA; 51572 MW; 48BBCB465036C161 CRC64; MSAKAAPQDY FVKDISLAEY GRKEIAIAET EMPGLMAARE EFGPSQPLKG ARICGSLHMT IQTAVLIQTL EALGAQVRWV SCNIYSTQDH AAAAIADAGT AVFAYKGETL EEYWDYTDRM FQWPDGEGPN LILDDGGDAT MYLILGEKAE SDPSFLEKPT SEEEKYFFAQ IKKRLTASPG WFKKTKAGVR GVSEETTTGV NRLYQLEKRG ELPFPAINVN DSVTKSKFDN KYGCKESLVD AIRRGTDVMM AGKKAFVAGY GDVGKGSAAS LAGSGARVGV SEVDPICALQ AAMDGFEVLT MDEAAPKFDI FVTATGNKDI LTVDHMRAMK DMAIVCNIGH FDNEIQVEGL RNFQWTNIKP QVDMITFPDG KRIILLSEGR LVNLGNATGH PSFVMSASFT NQTLAQIELH LRGNEYDNKV YTLPKHLDEK VARLHLDKLG VQLTKLSGEQ AAYIGVEQTG PFKPEHYRY //