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Database: UniProt
Entry: A0A2K6DCP1_MACNE
LinkDB: A0A2K6DCP1_MACNE
Original site: A0A2K6DCP1_MACNE 
ID   A0A2K6DCP1_MACNE        Unreviewed;       437 AA.
AC   A0A2K6DCP1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
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:ENSMNEP00000033672.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000033672.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000033672.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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}.
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DR   AlphaFoldDB; A0A2K6DCP1; -.
DR   STRING; 9545.ENSMNEP00000033672; -.
DR   Ensembl; ENSMNET00000058119.1; ENSMNEP00000033672.1; ENSMNEG00000040072.1.
DR   GeneTree; ENSGT00950000182981; -.
DR   OMA; YIGVTVE; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000040072; Expressed in liver and 12 other cell types or tissues.
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; 2.
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   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:UP000233120}.
FT   DOMAIN          203..357
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   BINDING         180..182
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         227..232
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         253
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         304..306
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         351
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         358
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ   SEQUENCE   437 AA;  47842 MW;  60F3E30F17647ED0 CRC64;
     MPHDAGAAAR AESRKRAACS VGEHTWPRPG TAADIGLAAW GRKALDIAEN EMPGLMRMRE
     QYSASKPLKG ARIAGCLHMT VETAVLIETL VALGAEVQWS SCNIFSTQDH AAAAIAKAGI
     PVYAWKGETD EEYLWCIEQT LYFKDGPLNM ILDDGGDLTN LIHTKYPQLL SGIRGISEET
     TTGVHNLYKM MANGILKVPA INSLIDGIKR ATDVMIAGKV AVVAGYGDVG KGCAQALRGF
     GACVIITEID PINALQAAME GYEVTTMDEA CQEGNIFVTT TGCVDIILGR HFEQMKDDAI
     VCNIGHFDVE IDVKWLNENA VEKVNIKPQV DRYRLKNGRR IILLAEGRLV NLGCAMGHPS
     FVMSNSFTNQ VMAQIELWTH PDKYPVGVHF LPKKLDEAVA EAHLGKLNVK LTKLTEKQAQ
     YLGMSRDGPF KPDHYRY
//
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