A0A0L0JTI1 · A0A0L0JTI1_9ACTN
- ProteinCarboxylic acid reductase
- Genecar
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1160 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the ATP- and NADPH-dependent reduction of carboxylic acids to the corresponding aldehydes.
Catalytic activity
- a carboxylate + ATP + H+ + NADPH = AMP + an aldehyde + diphosphate + NADP+
Cofactor
Note: Binds 1 phosphopantetheine covalently.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 307 | AMP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 402 | AMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 423-424 | AMP (UniProtKB | ChEBI) | ||||
Sequence: DG | ||||||
Binding site | 428 | AMP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 501 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 513-516 | AMP (UniProtKB | ChEBI) | ||||
Sequence: YVDR | ||||||
Binding site | 522 | AMP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 615 | AMP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 784-787 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: NGYL | ||||||
Binding site | 811 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 821 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 877-879 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: PAA | ||||||
Binding site | 917 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 948 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 952 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 975 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | NADP binding | |
Molecular Function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor | |
Molecular Function | phosphopantetheine binding | |
Biological Process | antibiotic biosynthetic process | |
Biological Process | lipid metabolic process | |
Biological Process | small molecule metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCarboxylic acid reductase
- EC number
- Short namesCAR
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A0L0JTI1
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 684 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 638-725 | Carrier | ||||
Sequence: RDQEDAVRVLRDEGAGRPVSETVERAARALLGSSAADARFTDLGGDSLSALSFSTLLAEIFGVEVPVGTVLSPANDLRALAAHIEARL |
Domain
The N-terminal domain likely catalyzes substrate activation by formation of an initial acyl-AMP intermediate, the central region contains the phosphopantetheine attachment site, and the C-terminal domain catalyzes the reduction by NADPH of the intermediate thioester formed from the attack of the phosphopantetheine thiol at the carbonyl carbon of acyl-AMP.
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,160
- Mass (Da)125,368
- Last updated2015-11-11 v1
- Checksum0A62461DD6A34D41
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JPPY01000183 EMBL· GenBank· DDBJ | KND28858.1 EMBL· GenBank· DDBJ | Genomic DNA |