| IED ID | IndEnz0015000007 |
| Enzyme Type ID | laccase000007 |
| Protein Name |
Purine nucleoside phosphorylase LACC1 EC 2.4.2.1 Adenosine deaminase LACC1 EC 3.5.4.4 Fatty acid metabolism-immunity nexus Guanosine phosphorylase LACC1 Laccase domain-containing protein 1 S-methyl-5'-thioadenosine phosphorylase LACC1 EC 2.4.2.28 |
| Gene Name | Lacc1 Famin |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MAEAVLIDLSGLQLNAQKNCHETLLETLDGIHYHHAPKAKFLCIICCRNASKEKDGEYGLCELEAGNGFSRLAGKFETVSHPCLAASLYTIKQKIDEENLSCIKVIVPEHRKLLMKAYVGQLFTEVYEFEFEDLQGAWRDSLLKPSTGINVTTTQELEDIQHEIETYLRSLPALKGDLTIVTSPLIPDNFLHGFTTRTGGISSVPTLSSLNLFSSSKRRDPKVVVQENVRRLANAAGFNAEKFYRIKTDHASEVWVMGKKEPESYDGIVTNQRGVTITALGADCIPIVFADPVKKACGVAHSGWKGTLLGVAMATVNAMIAEYGCDVEDIIVVLGPSVGSCCFTLPKESAVSFHSLHPSCVRHFDSPRPYVDIRKATRILLERGGILPQNIQDQKEDLDLCTSCHPEKFFSHVRDGLNFGTQIGFISLRE |
| Enzyme Length | 430 |
| Uniprot Accession Number | Q8BZT9 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:27642, ChEBI:CHEBI:16335, ChEBI:CHEBI:16708, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000250|UniProtKB:Q8IV20};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27643; Evidence={ECO:0000250|UniProtKB:Q8IV20}; CATALYTIC ACTIVITY: Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000250|UniProtKB:Q8IV20};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27647; Evidence={ECO:0000250|UniProtKB:Q8IV20}; CATALYTIC ACTIVITY: Reaction=guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine; Xref=Rhea:RHEA:13233, ChEBI:CHEBI:16235, ChEBI:CHEBI:16750, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000250|UniProtKB:Q8IV20};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13234; Evidence={ECO:0000250|UniProtKB:Q8IV20}; CATALYTIC ACTIVITY: Reaction=phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:11852, ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:43474, ChEBI:CHEBI:58533; EC=2.4.2.28; Evidence={ECO:0000250|UniProtKB:Q8IV20};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11853; Evidence={ECO:0000250|UniProtKB:Q8IV20}; CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000250|UniProtKB:Q8IV20};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409; Evidence={ECO:0000250|UniProtKB:Q8IV20}; |
| DNA Binding | |
| EC Number | 2.4.2.1; 3.5.4.4; 2.4.2.28 |
| Enzyme Function | FUNCTION: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine, guanosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine, guanine and hypoxanthine (By similarity). Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate (By similarity). Also has adenosine deaminase activity (By similarity). Acts as a regulator of innate immunity in macrophages by modulating the purine nucleotide metabolism, thereby regulating the metabolic function and bioenergetic state of macrophages (PubMed:27478939, PubMed:31978345). Enables a purine nucleotide cycle between adenosine and inosine monophosphate and adenylosuccinate that prevents cytoplasmic acidification and balances the cytoplasmic-mitochondrial redox interface (PubMed:31978345). The purine nucleotide cycle consumes aspartate and releases fumarate in a manner involving fatty acid oxidation and ATP-citrate lyase activity (PubMed:31978345). Participates in pattern recognition receptor-induced cytokines in macrophages: associates with the NOD2-signaling complex and promotes optimal NOD2-induced signaling, cytokine secretion and bacterial clearance (By similarity). Localizes to the endoplasmic reticulum upon PRR stimulation of macrophages and associates with endoplasmic reticulum-stress sensors, promoting the endoplasmic reticulum unfolded protein response (UPR) (By similarity). Does not show laccase activity (By similarity). {ECO:0000250|UniProtKB:Q8IV20, ECO:0000269|PubMed:27478939, ECO:0000269|PubMed:31978345}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (3); Modified residue (1); Mutagenesis (2) |
| Keywords | Acetylation;Cytoplasm;Endoplasmic reticulum;Hydrolase;Immunity;Inflammatory response;Innate immunity;Metal-binding;Nucleus;Peroxisome;Phosphoprotein;Reference proteome;Transferase;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30510070}. Nucleus {ECO:0000269|PubMed:30510070}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8IV20}. Peroxisome {ECO:0000250|UniProtKB:Q8IV20}. Note=Upon stimulation of the pattern-recognition receptor (PRR) NOD2, localizes to the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q8IV20}. |
| Modified Residue | MOD_RES 247; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q8IV20 |
| Post Translational Modification | PTM: Phosphorylated on tyrosine residues. {ECO:0000250|UniProtKB:Q8IV20}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12466851; 18799693; 21267068; 21677750; 32693188; 34986329; |
| Motif | |
| Gene Encoded By | |
| Mass | 47,514 |
| Kinetics | |
| Metal Binding | METAL 250; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P84138; METAL 284; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P84138; METAL 301; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P84138 |
| Rhea ID | RHEA:27642; RHEA:27643; RHEA:27646; RHEA:27647; RHEA:13233; RHEA:13234; RHEA:11852; RHEA:11853; RHEA:24408; RHEA:24409 |
| Cross Reference Brenda |