SAHH_MOUSE
ID SAHH_MOUSE Reviewed; 432 AA.
AC P50247; Q91WF1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Adenosylhomocysteinase;
DE Short=AdoHcyase;
DE EC=3.3.1.1 {ECO:0000269|PubMed:7657650};
DE AltName: Full=CUBP;
DE AltName: Full=Liver copper-binding protein;
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase;
GN Name=Ahcy;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7657650; DOI=10.1074/jbc.270.35.20698;
RA Bethin K.E., Petrovic N., Ettinger M.J.;
RT "Identification of a major hepatic copper binding protein as S-
RT adenosylhomocysteine hydrolase.";
RL J. Biol. Chem. 270:20698-20702(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-193, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the hydrolysis of S-adenosyl-L-homocysteine to form
CC adenosine and homocysteine (PubMed:7657650). Binds copper ions
CC (PubMed:7657650). {ECO:0000269|PubMed:7657650}.
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:0000269|PubMed:7657650};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21709;
CC Evidence={ECO:0000305|PubMed:7657650};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:7657650};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000269|PubMed:7657650};
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:7657650}.
CC -!- INTERACTION:
CC P50247; P39428: Traf1; NbExp=3; IntAct=EBI-646982, EBI-520123;
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; L32836; AAA70378.1; -; mRNA.
DR EMBL; BC015304; AAH15304.1; -; mRNA.
DR CCDS; CCDS16942.1; -.
DR RefSeq; NP_001291457.1; NM_001304528.1.
DR RefSeq; NP_057870.3; NM_016661.3.
DR PDB; 5AXA; X-ray; 1.55 A; A/C=1-432.
DR PDB; 5AXB; X-ray; 1.65 A; A/C=1-432.
DR PDB; 5AXC; X-ray; 1.55 A; A/C=1-432.
DR PDB; 5AXD; X-ray; 1.60 A; A/C=1-432.
DR PDBsum; 5AXA; -.
DR PDBsum; 5AXB; -.
DR PDBsum; 5AXC; -.
DR PDBsum; 5AXD; -.
DR AlphaFoldDB; P50247; -.
DR SMR; P50247; -.
DR BioGRID; 234644; 6.
DR IntAct; P50247; 3.
DR MINT; P50247; -.
DR STRING; 10090.ENSMUSP00000061851; -.
DR BindingDB; P50247; -.
DR ChEMBL; CHEMBL2389; -.
DR DrugCentral; P50247; -.
DR iPTMnet; P50247; -.
DR PhosphoSitePlus; P50247; -.
DR SwissPalm; P50247; -.
DR REPRODUCTION-2DPAGE; P50247; -.
DR EPD; P50247; -.
DR jPOST; P50247; -.
DR PaxDb; P50247; -.
DR PeptideAtlas; P50247; -.
DR PRIDE; P50247; -.
DR ProteomicsDB; 256586; -.
DR DNASU; 269378; -.
DR Ensembl; ENSMUST00000054607; ENSMUSP00000061851; ENSMUSG00000027597.
DR Ensembl; ENSMUST00000059524; ENSMUSP00000127198; ENSMUSG00000048087.
DR GeneID; 11615; -.
DR GeneID; 269378; -.
DR KEGG; mmu:11615; -.
DR KEGG; mmu:269378; -.
DR UCSC; uc008nka.2; mouse.
DR CTD; 11615; -.
DR CTD; 191; -.
DR MGI; MGI:87968; Ahcy.
DR VEuPathDB; HostDB:ENSMUSG00000027597; -.
DR VEuPathDB; HostDB:ENSMUSG00000048087; -.
DR eggNOG; KOG1370; Eukaryota.
DR GeneTree; ENSGT00950000182981; -.
DR HOGENOM; CLU_025194_2_1_1; -.
DR InParanoid; P50247; -.
DR OMA; NKYGCRE; -.
DR OrthoDB; 371693at2759; -.
DR PhylomeDB; P50247; -.
DR TreeFam; TF300415; -.
DR BRENDA; 3.3.1.1; 3474.
DR Reactome; R-MMU-156581; Methylation.
DR Reactome; R-MMU-1614635; Sulfur amino acid metabolism.
DR UniPathway; UPA00314; UER00076.
DR BioGRID-ORCS; 11615; 0 hits in 32 CRISPR screens.
DR BioGRID-ORCS; 269378; 22 hits in 74 CRISPR screens.
DR ChiTaRS; Ahcy; mouse.
DR PRO; PR:P50247; -.
DR Proteomes; UP000000589; Chromosome 16.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P50247; protein.
DR Bgee; ENSMUSG00000027597; Expressed in hindlimb bud and 125 other tissues.
DR ExpressionAtlas; P50247; baseline and differential.
DR Genevisible; P50247; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IDA:UniProtKB.
DR GO; GO:0030554; F:adenyl nucleotide binding; ISO:MGI.
DR GO; GO:0005507; F:copper ion binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IPI:MGI.
DR GO; GO:0002439; P:chronic inflammatory response to antigenic stimulus; ISO:MGI.
DR GO; GO:0042745; P:circadian sleep/wake cycle; ISO:MGI.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007584; P:response to nutrient; ISO:MGI.
DR GO; GO:0019510; P:S-adenosylhomocysteine catabolic process; IDA:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Copper; Cytoplasm; Hydrolase; Hydroxylation;
KW NAD; 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_0000116903"
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:0007744|PubMed:21183079"
FT CONFLICT 174
FT /note="K -> N (in Ref. 1; AAA70378)"
FT /evidence="ECO:0000305"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:5AXA"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:5AXA"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:5AXA"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:5AXA"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:5AXA"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5AXA"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:5AXA"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:5AXA"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 190..207
FT /evidence="ECO:0007829|PDB:5AXA"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 223..234
FT /evidence="ECO:0007829|PDB:5AXA"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:5AXA"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:5AXA"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:5AXA"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:5AXA"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 308..314
FT /evidence="ECO:0007829|PDB:5AXA"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:5AXA"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:5AXA"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 345..349
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 355..374
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:5AXA"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 388..396
FT /evidence="ECO:0007829|PDB:5AXA"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:5AXA"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:5AXA"
SQ SEQUENCE 432 AA; 47688 MW; 15CCD20B7088D5CA CRC64;
MSDKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMREMYS ASKPLKGARI AGCLHMTVET
AVLIETLVAL GAEVRWSSCN IFSTQDHAAA AIAKAGIPVF AWKGETDEEY LWCIEQTLHF
KDGPLNMILD DGGDLTNLIH TKYPQLLSGI RGISEETTTG VHNLYKMMSN GILKVPAINV
NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI
ITEIDPINAL QAAMEGYEVT TMDEACKEGN IFVTTTGCVD IILGRHFEQM KDDAIVCNIG
HFDVEIDVKW LNENAVEKVN IKPQVDRYWL KNGRRIILLA EGRLVNLGCA MGHPSFVMSN
SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG KLNVKLTKLT EKQAQYLGMP
INGPFKPDHY RY
