GenomeNet

Database: UniProt
Entry: Q4R596
LinkDB: Q4R596
Original site: Q4R596 
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   29-OCT-2014, entry version 55.
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. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = L-
CC       homocysteine + adenosine.
CC   -!- COFACTOR: Binds 1 NAD per subunit. {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB169648; BAE01729.1; -; mRNA.
DR   RefSeq; NP_001270215.1; NM_001283286.1.
DR   UniGene; Mfa.8296; -.
DR   ProteinModelPortal; Q4R596; -.
DR   SMR; Q4R596; 3-432.
DR   PRIDE; Q4R596; -.
DR   GeneID; 101865247; -.
DR   KEGG; mcf:101865247; -.
DR   CTD; 191; -.
DR   HOVERGEN; HBG005041; -.
DR   KO; K01251; -.
DR   UniPathway; UPA00314; UER00076.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; -; 1.
DR   HAMAP; MF_00563; AdoHcyase; 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. {ECO:0000250}.
FT   CHAIN         2    432       Adenosylhomocysteinase.
FT                                /FTId=PRO_0000260218.
FT   REGION      183    350       NAD binding. {ECO:0000250}.
FT   BINDING      57     57       Substrate. {ECO:0000250}.
FT   BINDING     131    131       Substrate. {ECO:0000250}.
FT   BINDING     156    156       Substrate. {ECO:0000250}.
FT   BINDING     186    186       Substrate. {ECO:0000250}.
FT   BINDING     190    190       Substrate. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylserine. {ECO:0000250}.
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
//
DBGET integrated database retrieval system