ID   SAHH_BOVIN              Reviewed;         432 AA.
AC   Q3MHL4; A5D9B8;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 35.
DE   RecName: Full=Adenosylhomocysteinase;
DE            Short=AdoHcyase;
DE            EC=3.3.1.1;
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase;
GN   Name=AHCY;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Adenosylhomocysteine is a competitive inhibitor of S-
CC       adenosyl-L-methionine-dependent methyl transferase reactions;
CC       therefore adenosylhomocysteinase may play a key role in the
CC       control of methylations via regulation of the intracellular
CC       concentration of adenosylhomocysteine (By similarity).
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   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
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DR   EMBL; BT030537; ABQ12977.1; -; mRNA.
DR   EMBL; BC105194; AAI05195.1; -; mRNA.
DR   IPI; IPI00714294; -.
DR   RefSeq; NP_001029487.1; -.
DR   UniGene; Bt.12322; -.
DR   SMR; Q3MHL4; 3-432.
DR   Ensembl; ENSBTAG00000018101; Bos taurus.
DR   GeneID; 508158; -.
DR   KEGG; bta:508158; -.
DR   HOVERGEN; Q3MHL4; -.
DR   OMA; Q3MHL4; HMRAMKD.
DR   BRENDA; 3.3.1.1; 251.
DR   GO; GO:0005829; C:cytosol; ISS:AgBase.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; ISS:AgBase.
DR   GO; GO:0005507; F:copper ion binding; ISS:AgBase.
DR   GO; GO:0043621; F:protein self-association; ISS:AgBase.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019510; P:S-adenosylhomocysteine catabolic process; ISS:AgBase.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Hydrolase; NAD; One-carbon metabolism.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    432       Adenosylhomocysteinase.
FT                                /FTId=PRO_0000260217.
FT   REGION      183    350       NAD binding (By similarity).
FT   BINDING      57     57       Substrate (By similarity).
FT   BINDING     131    131       Substrate (By similarity).
FT   BINDING     156    156       Substrate (By similarity).
FT   BINDING     186    186       Substrate (By similarity).
FT   BINDING     190    190       Substrate (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
SQ   SEQUENCE   432 AA;  47638 MW;  314540823FA21BAB CRC64;
     MSDKLPYKVA DISLAAWGRK ALDLAENEMP GLMHMREMYS ASKPLKGARI AGCLHMTVET
     AVLIETLVAL GAEVRWSSCN IFSTQDHAAA AIAKAGIPVY AWKGETDEEY LWCIEQTLYF
     KDGPLNMILD DGGDLTNLIH TKYPQLLSGI RGISEETTTG VHNLYKMMAK GILKVPAINV
     NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI
     ITEIDPINAL QAAMEGYEVT TMDEACQEGN IFVTTTGCTD IILGQHFEQM KDDAIVCNIG
     HFDVEIDVKW LNENAVEKVN IKPQVDRYLL KNGRRIILLA EGRLVNLGCA MGHPSFVMSN
     SFTNQVLAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG KLNVKLTKLT EKQAQYLGVS
     REGPFKPDHY RY
//