SAHH_BOVIN
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 03-AUG-2022, entry version 120.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC 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: 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT030537; ABQ12977.1; -; mRNA.
DR EMBL; BC105194; AAI05195.1; -; mRNA.
DR RefSeq; NP_001029487.1; NM_001034315.1.
DR AlphaFoldDB; Q3MHL4; -.
DR SMR; Q3MHL4; -.
DR STRING; 9913.ENSBTAP00000024092; -.
DR PaxDb; Q3MHL4; -.
DR PeptideAtlas; Q3MHL4; -.
DR PRIDE; Q3MHL4; -.
DR Ensembl; ENSBTAT00000024092; ENSBTAP00000024092; ENSBTAG00000018101.
DR GeneID; 508158; -.
DR KEGG; bta:508158; -.
DR CTD; 191; -.
DR VEuPathDB; HostDB:ENSBTAG00000018101; -.
DR VGNC; VGNC:25750; AHCY.
DR eggNOG; KOG1370; Eukaryota.
DR GeneTree; ENSGT00950000182981; -.
DR HOGENOM; CLU_025194_2_1_1; -.
DR InParanoid; Q3MHL4; -.
DR OMA; NKYGCRE; -.
DR OrthoDB; 371693at2759; -.
DR TreeFam; TF300415; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000018101; Expressed in liver and 104 other tissues.
DR ExpressionAtlas; Q3MHL4; baseline and differential.
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: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 2: Evidence at transcript level;
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_0000260217"
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"
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
