AC MF_03018; DC Protein; auto c? TR HAMAP; MF_01971; -; 1; level=0 XX Names: Kynurenine_monooxygenase_euk XX ID KMO case DE RecName: Full=Kynurenine 3-monooxygenase; DE EC=1.14.13.9; DE AltName: Full=Biosynthesis of nicotinic acid protein 4; DE AltName: Full=Kynurenine 3-hydroxylase; else DE RecName: Full=Kynurenine 3-monooxygenase; DE EC=1.14.13.9; DE AltName: Full=Kynurenine 3-hydroxylase; end case case GN Name=kmo; else case GN Name=cn; else case GN Name=BNA4; else case and not and not GN Name=KMO; end case XX case CC -!- FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form CC 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic CC acid, a neurotoxic NMDA receptor antagonist and potential endogenous CC inhibitor of NMDA receptor signaling in axonal targeting, CC synaptogenesis and apoptosis during brain development. Quinolinic acid CC may also affect NMDA receptor signaling in pancreatic beta cells, CC osteoblasts, myocardial cells, and the gastrointestinal tract. else CC -!- FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form CC 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic CC acid. end case CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + CC H2O + NADP(+); Xref=Rhea:RHEA:20545, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:57959, ChEBI:CHEBI:58125, ChEBI:CHEBI:58349; CC EC=1.14.13.9; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from CC L-kynurenine: step 1/3. case CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane CC protein. else case or CC -!- SUBCELLULAR LOCATION: Mitochondrion. Membrane; Multi-pass membrane CC protein. else case CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane. else CC -!- SUBCELLULAR LOCATION: Mitochondrion. end case CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO CC subfamily. XX DR Pfam; PF01266; DAO; 1; trigger=no DR PRINTS; PR00420; RNGMNOXGNASE; 1; trigger=no XX KW FAD KW Flavoprotein KW Mitochondrion case or or or KW Membrane end case case or KW Mitochondrion outer membrane end case KW Monooxygenase KW NADP KW Oxidoreductase KW Pyridine nucleotide biosynthesis case KW Transmembrane KW Transmembrane helix end case XX GO GO:0004502; F:kynurenine 3-monooxygenase activity GO GO:0050660; F:flavin adenine dinucleotide binding GO GO:0006569; P:tryptophan catabolic process GO GO:0019805; P:quinolinate biosynthetic process GO GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan GO GO:0043420; P:anthranilate metabolic process case or or or GO GO:0031966; C:mitochondrial membrane else GO GO:0005739; C:mitochondrion end case XX FT From: KMO_HUMAN (O15229) case FT TRANSMEM 385..404 FT /note="Helical" FT Tag: transmembrane FT TRANSMEM 425..445 FT /note="Helical" FT Tag: transmembrane end case FT From: KMO_DROME (A1Z746) case FT TRANSMEM 405..427 FT /note="Helical" FT Tag: transmembrane FT TRANSMEM 440..462 FT /note="Helical" FT Tag: transmembrane end case FT From: KMO_CAEBR (A8Y432) case FT TRANSMEM 395..415 FT /note="Helical" FT Tag: transmembrane FT TRANSMEM 432..452 FT /note="Helical" FT Tag: transmembrane end case XX Size: 427-600; Related: None; Template: O15229; Q91WN4; O88867; Q86PM2; P38169; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: in ASPNC Plasmid: None Comments: None XX # Revision 1.14 2019/11/20 //