ID SAHH_MACFA Reviewed; 432 AA.
AC Q4R596;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 06-MAR-2013, entry version 47.
DE RecName: Full=Adenosylhomocysteinase;
DE Short=AdoHcyase;
DE EC=3.3.1.1;
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase;
GN Name=AHCY; ORFNames=QccE-12261;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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; L-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; AB169648; BAE01729.1; -; mRNA.
DR HSSP; P23526; 1LI4.
DR ProteinModelPortal; Q4R596; -.
DR SMR; Q4R596; 3-432.
DR PRIDE; Q4R596; -.
DR HOVERGEN; HBG005041; -.
DR UniPathway; UPA00314; UER00076.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR000043; Adenosylhomocysteinase.
DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR PANTHER; PTHR23420; PTHR23420; 1.
DR Pfam; PF05221; AdoHcyase; 1.
DR Pfam; PF00670; AdoHcyase_NAD; 1.
DR PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1.
DR SMART; SM00996; AdoHcyase; 1.
DR SMART; SM00997; AdoHcyase_NAD; 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_0000260218.
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; 47687 MW; 65B53F02612D934E CRC64;
MSDKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMREQYS ASKPLKGARI AGCLHMTVET
AVLIETLVAL GAEVQWSSCN IFSTQDHAAA AIAKAGIPVY AWKGETDEEY LWCIEQTLYF
KDGPLNMILD DGGDLTNLIH TKYPQLLSGI RGISEETTTG VHNLYKMMAN GILKVPAINV
NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI
ITEIDPINAL QAAMEGYEVT TMDEACQEGN IFVTTTGCVD IILGRHFEQM KDDAIVCNIG
HFDVEIDVKW LNENAVEKVN IKPQVDRYRL KNGRRIILLA EGRLVNLGCA MGHPSFVMSN
SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG KLNVKLTKLT EKQAQYLGMS
RDGPFKPDHY RY
//
