B1VMZ4 · B1VMZ4_STRGG
- ProteinCarboxylic acid reductase
- Genecar
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1148 (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 + NADPH + H+ = an aldehyde + AMP + diphosphate + NADP+
Cofactor
Note: Binds 1 phosphopantetheine covalently.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 276 | AMP (UniProtKB | ChEBI) | |||
Binding site | 368 | AMP (UniProtKB | ChEBI) | |||
Binding site | 394 | AMP (UniProtKB | ChEBI) | |||
Binding site | 467 | AMP (UniProtKB | ChEBI) | |||
Binding site | 479-482 | AMP (UniProtKB | ChEBI) | |||
Binding site | 488 | AMP (UniProtKB | ChEBI) | |||
Binding site | 590 | AMP (UniProtKB | ChEBI) | |||
Binding site | 763-766 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 790 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 800 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 856-858 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 896 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 932 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 936 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 959 | NADP+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | ATP binding | |
Molecular Function | long-chain fatty acid-CoA ligase activity | |
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 |
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
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionB1VMZ4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 663 | O-(pantetheine 4'-phosphoryl)serine | |||
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 629-704 | Carrier | |||
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
- Length1,148
- Mass (Da)123,158
- Last updated2008-05-20 v1
- MD5 Checksum7E247579D5B9A0A7480C26ED9AB6E4CC
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP009493 EMBL· GenBank· DDBJ | BAG23619.1 EMBL· GenBank· DDBJ | Genomic DNA |