ID   SAHH_BACTN              Reviewed;         476 AA.
AC   Q8A407;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 45.
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=BT_2797;
OS   Bacteroides thetaiotaomicron.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
RX   MEDLINE=22550858; PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
RA   Chiang H.C., Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO77903.1; -; Genomic_DNA.
DR   RefSeq; NP_811709.1; -.
DR   HSSP; P23526; 1LI4.
DR   GeneID; 1072485; -.
DR   GenomeReviews; AE015928_GR; BT_2797.
DR   KEGG; bth:BT_2797; -.
DR   NMPDR; fig|226186.1.peg.2796; -.
DR   HOGENOM; Q8A407; -.
DR   OMA; Q8A407; HMRAMKD.
DR   BioCyc; BTHE226186:BT_2797-MON; -.
DR   BRENDA; 3.3.1.1; 21018.
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    476       Adenosylhomocysteinase.
FT                                /FTId=PRO_0000116943.
FT   REGION      228    396       NAD binding (By similarity).
FT   BINDING      65     65       Substrate (By similarity).
FT   BINDING     140    140       Substrate (By similarity).
FT   BINDING     201    201       Substrate (By similarity).
FT   BINDING     231    231       Substrate (By similarity).
FT   BINDING     235    235       Substrate (By similarity).
SQ   SEQUENCE   476 AA;  52739 MW;  4D11030800F2E163 CRC64;
     MIYNMSTELF STLPYKVADI TLADFGRKEI DLAEKEMPGL MALREKYGES KPLKGARIMG
     SLHMTIQTAV LIETLVALGA EVRWCSCNIY STQDHAAAAI AASGVAVFAW KGENLADYWW
     CTLQALNFPG GKGPNVIVDD GGDATMMIHV GYDAENDAAV LDKEVHAEDE IELNAILKKV
     LAEDKTRWHR VAEEMRGVSE ETTTGVHRLY QMQEEGKLLF PAFNVNDSVT KSKFDNLYGC
     RESLADGIKR ATDVMIAGKV VVVCGYGDVG KGCSHSMRSY GARVLVTEVD PICALQAAME
     GFEVVTMEDA CTEGNIFVTT TGNIDIIRID HMEKMKDQAI VCNIGHFDNE IQVDALKHYS
     GIKCVNIKPQ VDRYYFPDGH SILLLADGRL VNLGCATGHP SFVMSNSFTN QTLAQIELFN
     KKYEVNVYRL PKHLDEEVAR LHLEKIGVKL TKLTPEQAAY IGVSVDGPYK AEHYRY
//