AC MF_02247; DC Protein; auto TR HAMAP; MF_02247; -; 1; level=0 XX Names: Carbox_acid_reduct XX ID CAR DE RecName: Full=Carboxylic acid reductase; DE Short=CAR; DE EC=1.2.1.-; DE AltName: Full=ATP/NADPH-dependent carboxylic acid reductase; GN Name=car; XX CC -!- FUNCTION: Catalyzes the ATP- and NADPH-dependent reduction of CC carboxylic acids to the corresponding aldehydes. CC -!- CATALYTIC ACTIVITY: CC Reaction=a carboxylate + ATP + H(+) + NADPH = AMP + an aldehyde + CC diphosphate + NADP(+); Xref=Rhea:RHEA:50916, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:456215; CC -!- COFACTOR: CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; CC Note=Binds 1 phosphopantetheine covalently.; CC -!- DOMAIN: The N-terminal domain likely catalyzes substrate activation by CC formation of an initial acyl-AMP intermediate, the central region CC contains the phosphopantetheine attachment site, and the C-terminal CC domain catalyzes the reduction by NADPH of the intermediate thioester CC formed from the attack of the phosphopantetheine thiol at the carbonyl CC carbon of acyl-AMP. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. CC Carboxylic acid reductase subfamily. XX DR PROSITE; PS00455; AMP_BINDING; 1; trigger=no DR PROSITE; PS50075; CARRIER; 1; trigger=yes DR Pfam; PF00501; AMP-binding; 1; trigger=no DR Pfam; PF00550; PP-binding; 1; trigger=no DR Pfam; PF07993; NAD_binding_4; 1; trigger=no DR NCBIfam; TIGR01746; Thioester-redct; 1; trigger=no XX KW ATP-binding KW NADP KW Nucleotide-binding KW Oxidoreductase KW Phosphopantetheine KW Phosphoprotein XX GO GO:0005524; F:ATP binding GO GO:0050661; F:NADP binding GO GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor GO GO:0031177; F:phosphopantetheine binding XX FT From: CAR_SEGRC (E5XP76) FT BINDING 429..430 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Optional; Condition: [DE]-G FT BINDING 519..522 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Optional; Condition: Y-[VL]-D-R FT BINDING 801..804 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Optional; Condition: [NT]-G-[FYW]-L FT BINDING 868..869 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Optional; Condition: D-[FK] FT BINDING 894..896 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Optional; Condition: [SP]-[GA]-A FT BINDING 315 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Optional; Condition: H FT BINDING 408 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Optional; Condition: [ST] FT BINDING 434 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Optional; Condition: T FT BINDING 507 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Optional; Condition: D FT BINDING 528 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Optional; Condition: K FT BINDING 629 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Optional; Condition: K FT BINDING 828 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Optional; Condition: R FT BINDING 838 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Optional; Condition: R FT BINDING 934 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Optional; Condition: S FT BINDING 970 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Optional; Condition: Y FT BINDING 974 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Optional; Condition: K FT BINDING 997 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Optional; Condition: S FT MOD_RES 702 FT /note="O-(pantetheine 4'-phosphoryl)serine" FT Condition: S XX Size: 1000-1250; Related: None; Template: B2HN69; Q6RKB1; E5XP76; Scope: Bacteria; Actinomycetota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.5 2023/06/01 //