AC MF_02097; DC Protein; auto TR HAMAP; MF_02097; -; 1; level=0 XX Names: Carnitine_monoox_A XX ID CNTA DE RecName: Full=Carnitine monooxygenase oxygenase subunit; DE EC=1.14.13.239; DE AltName: Full=Carnitine monooxygenase alpha subunit; XX CC -!- FUNCTION: Converts carnitine to trimethylamine and malic semialdehyde. CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-carnitine + H(+) + NADH + O2 = (3R)-3-hydroxy-4- CC oxobutanoate + H2O + NAD(+) + trimethylamine; Xref=Rhea:RHEA:55396, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:58389, ChEBI:CHEBI:138809; EC=1.14.13.239; CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-carnitine + H(+) + NADPH + O2 = (3R)-3-hydroxy-4- CC oxobutanoate + H2O + NADP(+) + trimethylamine; Xref=Rhea:RHEA:55368, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:58389, ChEBI:CHEBI:138809; EC=1.14.13.239; case CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Note=Binds 1 [2Fe-2S] cluster per subunit.; end case CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Note=Binds 1 Fe cation per subunit CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism. CC -!- SUBUNIT: Composed of an oxygenase subunit and a reductase subunit. CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase CC alpha subunit family. CntA subfamily. XX DR PROSITE; PS51296; RIESKE; 1; trigger=yes DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1; trigger=no DR Pfam; PF00355; Rieske; 1; trigger=no DR Pfam; PF00848; Ring_hydroxyl_A; 1; trigger=no DR PRINTS; PR00090; RNGDIOXGNASE; 1; trigger=no XX case KW 2Fe-2S KW Iron-sulfur end case KW Iron KW Metal-binding KW NAD KW NADP KW Oxidoreductase XX GO GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen case GO GO:0051537; F:2 iron, 2 sulfur cluster binding end case XX FT From: CNTA_ACIB2 (D0C9N6) FT BINDING 86 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT Group: 1; Condition: C FT BINDING 88 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT Group: 1; Condition: H FT BINDING 106 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT Group: 1; Condition: C FT BINDING 109 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT Group: 1; Condition: H FT BINDING 208 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Condition: H FT BINDING 213 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Condition: H FT BINDING 323 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Condition: D XX Size: 365-405; Related: None; Template: D0C9N6; F0KFI5; P0ABR7; Scope: Bacteria; Pseudomonadota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: See MF_02098 for the reductase subunit. XX # Revision 1.8 2023/01/26 //