ID   SAHH_LEPBJ              Reviewed;         436 AA.
AC   Q04NN6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=LBJ_4089;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A.,
RA   Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P.,
RA   Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(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.
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DR   EMBL; CP000351; ABJ77484.1; -; Genomic_DNA.
DR   RefSeq; YP_802242.1; -.
DR   GeneID; 4412366; -.
DR   GenomeReviews; CP000351_GR; LBJ_4089.
DR   KEGG; lbj:LBJ_4089; -.
DR   OMA; Q04NN6; 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    436       Adenosylhomocysteinase.
FT                                /FTId=PRO_1000024729.
FT   REGION      188    356       NAD binding (By similarity).
FT   BINDING      62     62       Substrate (By similarity).
FT   BINDING     136    136       Substrate (By similarity).
FT   BINDING     161    161       Substrate (By similarity).
FT   BINDING     191    191       Substrate (By similarity).
FT   BINDING     195    195       Substrate (By similarity).
SQ   SEQUENCE   436 AA;  48096 MW;  F4BD8B927CAFC3E1 CRC64;
     MSATTQEKGL NYKVKDLSQA EWGRQEIILA EKEMPGLMAL RQEYKGKKPL AGARIAGSLH
     MTIQTAVLIE TLTELGAEVR WSSCNIFSTQ DHAAAAIAKA GVPVFAWKGE TEEEYWWCIE
     QTLFFGDKGP NMILDDGGDL TAYVHEKYPK LLSEIRGISE ETTTGVKSLY KLLKKGELKV
     PAFNVNDSVT KSKFDNLYGC RESLADGIKR ATDVMLAGKV ALVCGFGDVG KGSAASLRNF
     GARVIVTEID PICALQASME GYQVLRVEDI IEQVDIVVTA TGNDDIITLE HMKAMKDGAI
     LCNIGHFDTE IQMSRLNSEK GVTKKEIKPQ VDKYTFPDGK SIVVLAEGRL VNLGCATGHP
     SFVMSCSFTN QVLAQIELYN NKYELGVYTL PKHLDEKVAA LHLEQLGVRL TKLNQKQADY
     LGVPLNGPFK PENYRY
//