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
