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SAHH_PIG
ID   SAHH_PIG                Reviewed;         432 AA.
AC   Q710C4; Q4R1H7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Adenosylhomocysteinase;
DE            Short=AdoHcyase;
DE            EC=3.3.1.1 {ECO:0000250|UniProtKB:P10760};
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase;
GN   Name=AHCY;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12438749; DOI=10.1159/000064066;
RA   Leeb T., Rohrer G.A.;
RT   "Characterization and chromosomal assignment of the porcine AHCY gene for
RT   S-adenosylhomocysteine hydrolase.";
RL   Cytogenet. Genome Res. 97:116-119(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Okumura N., Nii M., Hamasima N.;
RT   "Expression of agouti signaling protein gene (ASIP) in pig.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of S-adenosyl-L-homocysteine to form
CC       adenosine and homocysteine (By similarity). Binds copper ions (By
CC       similarity). {ECO:0000250|UniProtKB:P10760,
CC       ECO:0000250|UniProtKB:P50247}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC         Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.3.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P10760};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21709;
CC         Evidence={ECO:0000250|UniProtKB:P10760};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000250|UniProtKB:P10760};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000250|UniProtKB:P10760};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P10760}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23526}.
CC       Melanosome {ECO:0000250|UniProtKB:P23526}.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ427478; CAD20603.1; -; Genomic_DNA.
DR   EMBL; AB206998; BAD99576.1; -; Genomic_DNA.
DR   RefSeq; NP_001011727.1; NM_001011727.1.
DR   AlphaFoldDB; Q710C4; -.
DR   SMR; Q710C4; -.
DR   STRING; 9823.ENSSSCP00000007750; -.
DR   PaxDb; Q710C4; -.
DR   PeptideAtlas; Q710C4; -.
DR   PRIDE; Q710C4; -.
DR   GeneID; 497050; -.
DR   KEGG; ssc:497050; -.
DR   CTD; 191; -.
DR   eggNOG; KOG1370; Eukaryota.
DR   HOGENOM; CLU_025194_2_1_1; -.
DR   InParanoid; Q710C4; -.
DR   OrthoDB; 371693at2759; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; Q710C4; SS.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; ISS:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central.
DR   CDD; cd00401; SAHH; 1.
DR   Gene3D; 3.40.50.1480; -; 3.
DR   HAMAP; MF_00563; AdoHcyase; 1.
DR   InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR   InterPro; IPR000043; Adenosylhomocysteinase-like.
DR   InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00936; ahcY; 1.
DR   PROSITE; PS00738; ADOHCYASE_1; 1.
DR   PROSITE; PS00739; ADOHCYASE_2; 1.
PE   3: Inferred from homology;
KW   Acetylation; Copper; Cytoplasm; Hydrolase; Hydroxylation; NAD;
KW   One-carbon metabolism; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P23526"
FT   CHAIN           2..432
FT                   /note="Adenosylhomocysteinase"
FT                   /id="PRO_0000116904"
FT   REGION          183..350
FT                   /note="NAD binding"
FT                   /evidence="ECO:0000250|UniProtKB:P10760"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10760"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10760"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10760"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10760"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10760"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23526"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23526"
FT   MOD_RES         186
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P23526"
FT   MOD_RES         193
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P50247"
FT   CONFLICT        41
FT                   /note="A -> T (in Ref. 2; BAD99576)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   432 AA;  47694 MW;  0B756B5F83F6B90E CRC64;
     MSEKLPYKVA DISLAAWGRK ALDLAENEMP GLMRMREMYS ASKPLKGARI AGCLHMTVET
     AVLIETLVAL GAEVRWSSCN IFSTQDHAAA AIAKAGIPVY AWKGETDEEY LWCIEQTLYF
     KDGPLNMILD DGGDLTNLVH TKYPELLSGI RGISEETTTG VHNLYKMKAN GILKVPAINV
     NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI
     ITEIDPINAL QAAMEGYEVT TMDEACQEGN IFVTTTGCID IILGRHFEQM KDDAIVCNIG
     HFDVEIDVKW LNENAVEKVN IKPQVDRYLL KNGHRIILLA EGRLVNLGCA MGHPSFVMSN
     SFTNQVLAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG KLNVKLTKLT EKQAQYLGMS
     REGPFKPDHY RY
 
 
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