ID M3Z294_MUSPF Unreviewed; 432 AA.
AC M3Z294;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Adenosylhomocysteinase {ECO:0000256|ARBA:ARBA00022091};
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000256|ARBA:ARBA00033091};
GN Name=AHCY {ECO:0000313|Ensembl:ENSMPUP00000017706.1,
GN ECO:0000313|RefSeq:XP_004746662.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000017706.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000017706.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004746662.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004746662.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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=3.13.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00036565};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21709;
CC Evidence={ECO:0000256|ARBA:ARBA00036565};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|PIRSR:PIRSR001109-2};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|PIRSR:PIRSR001109-2};
CC -!- SUBUNIT: Homotetramer. Interaction with AHCYL1.
CC {ECO:0000256|ARBA:ARBA00038791}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000256|ARBA:ARBA00007122, ECO:0000256|RuleBase:RU004166}.
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DR EMBL; AEYP01020712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004746662.1; XM_004746605.3.
DR STRING; 9669.ENSMPUP00000017706; -.
DR Ensembl; ENSMPUT00000017966.1; ENSMPUP00000017706.1; ENSMPUG00000017817.1.
DR GeneID; 101680234; -.
DR KEGG; mpuf:101680234; -.
DR CTD; 191; -.
DR eggNOG; KOG1370; Eukaryota.
DR GeneTree; ENSGT00950000182981; -.
DR HOGENOM; CLU_025194_2_1_1; -.
DR OMA; YIGVTVE; -.
DR OrthoDB; 120477at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:Ensembl.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 3.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 NCBIfam; TIGR00936; ahcY; 1.
DR PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 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; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00738; ADOHCYASE_1; 1.
DR PROSITE; PS00739; ADOHCYASE_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR001109-2};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715}.
FT DOMAIN 191..352
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 157..159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 222..227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 299..301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 346
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 353
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 432 AA; 47767 MW; F946A59909FAD7DC CRC64;
MSDKLPYKVA DISLASWGRK ALDIAENEMP GLMRMREMYS ASKPLKGARI AGCLHMTVET
AVLIETLVAL GAEVQWSSCN IFSTQDHAAA AIAKAGIPVY AWKGETDEEY LWCIEQTLYF
KDGPLNMILD DGGDLTNLIH TKYPQLLSGI RGISEETTTG VHNLYKMMAN GKLKVPAINV
NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI
ITEIDPINAL QAAMEGYEVT TMDEACQEGN IFVTTTGCTD IILGRHFEQM KDDSIVCNIG
HFDVEIDVKW LNENAVEKVN IKPQVDRYWL KNGRRIILLA EGRLVNLGCA TGHPSFVMSN
SFTNQVLAQI ELWTHPDKYS VGVHFLPKKL DEAVAEAHLT KLNVKLTKLT EKQAQYLGLS
RDGPFKPDHY RY
//
