ID   SAHH_MARMM              Reviewed;         469 AA.
AC   Q0ALW1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=Mmar10_2440;
OS   Maricaulis maris (strain MCS10).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Maricaulis.
OX   NCBI_TaxID=394221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Viollier P., Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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.
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DR   EMBL; CP000449; ABI66732.1; -; Genomic_DNA.
DR   RefSeq; YP_757670.1; -.
DR   GeneID; 4285422; -.
DR   GenomeReviews; CP000449_GR; Mmar10_2440.
DR   KEGG; mmr:Mmar10_2440; -.
DR   NMPDR; fig|394221.5.peg.2393; -.
DR   HOGENOM; Q0ALW1; -.
DR   OMA; Q0ALW1; HMRAMKD.
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_1000061127.
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;  51834 MW;  132FEE516538AE35 CRC64;
     MTQFAADKPY IVKDMSLAKW GRIEFDMAEI EMPGLMALRE EYKDSQPLKG ARIAGSLHMT
     VQTAILIETL TALGAEVRWA SCNIFSTQDH AAAAIAETGV PVFATKGETL EEYWDYADAI
     FHWPDGETAN MILDDGGDAT MYLILGEKAE NDPSVLNHPK SEEETFLFAQ IKKRIAATPG
     WFAKAKAAIQ GVSEETTTGV MRLYQMQKRG ELPFPAINVN DSVTKSKFDN RYGCRESLVD
     AIRRGTDVMM AGKKALVFGY GDVGKGSAES LAGAGARVYV TEIDPICALQ ACMDGFEVVR
     AEDVIGEMDI FVTATGNKDI LTVDHMRAMK DMAIVCNIGH FDNEIQVESL KNYQWTNVKP
     QVDLVNFPEG HRIILLSEGR LVNLGNATGH PSFVMSASFT NQTLAQIELW TKGENYTNEV
     YILPKHLDEK VAALHLDKLG AKLTVLSDEQ ADYIGVPQHG PFKAEHYRY
//