ID   SAHH_CHLTE              Reviewed;         471 AA.
AC   Q8KEG8;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 47.
DE   RecName: Full=Adenosylhomocysteinase;
DE            EC=3.3.1.1;
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase;
DE            Short=AdoHcyase;
GN   Name=ahcY; Synonyms=sahH; OrderedLocusNames=CT0721;
OS   Chlorobium tepidum.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=1097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM71958.1; -; Genomic_DNA.
DR   RefSeq; NP_661616.1; -.
DR   HSSP; P10760; 1B3R.
DR   GeneID; 1006351; -.
DR   GenomeReviews; AE006470_GR; CT0721.
DR   KEGG; cte:CT0721; -.
DR   NMPDR; fig|194439.1.peg.710; -.
DR   TIGR; CT0721; -.
DR   HOGENOM; Q8KEG8; -.
DR   OMA; Q8KEG8; HMRAMKD.
DR   BioCyc; CTEP194439:CT_0721-MON; -.
DR   BRENDA; 3.3.1.1; 189605.
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    471       Adenosylhomocysteinase.
FT                                /FTId=PRO_0000116956.
FT   REGION      223    391       NAD binding (By similarity).
FT   BINDING      60     60       Substrate (By similarity).
FT   BINDING     135    135       Substrate (By similarity).
FT   BINDING     196    196       Substrate (By similarity).
FT   BINDING     226    226       Substrate (By similarity).
FT   BINDING     230    230       Substrate (By similarity).
SQ   SEQUENCE   471 AA;  51949 MW;  31B082405D241047 CRC64;
     MTTEAAVLDY KVADISLAEW GRKEIEIAEK EMPGLMATRK KYEGKKPLAG ARIAGSLHMT
     IQTAVLIETL VELGADVRWA SCNIFSTQDH AAAAIAAAGV PVFAWKGETL DEYWWCTRQI
     LEFEGGLGPN LIVDDGGDAT LMIHFGYKIE NDPSMLDKTP GNAEEKALLQ QLKAVFAEDN
     QRWHKVAAGM KGVSEETTTG VHRLYQMMEK GELLFPAINV NDSVTKSKFD NLYGCRESLA
     DGIKRATDVM IAGKVVVVLG YGDVGKGCAH SMRSYGARVI VTEIDPICAL QAAMEGFEVT
     TMEEAVKEGN IFVTATGNKD VITLDHIKQM RDEAIVCNIG HFDNEIQVDA LNNFKGATRI
     NIKPQVDKYV FENGNCIYLL AEGRLVNLGC ATGHPSFVMS NSFTNQTLAQ IELWQNDYKV
     GVYRLPKKLD EEVARLHLGQ IGAKLTTLTK EQADYIGVPV EGPYKPEHYR Y
//