E5XP76 · CAR_SEGRC
- ProteinCarboxylic acid reductase
- Genecar
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1188 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the ATP- and NADPH-dependent reduction of carboxylic acids to the corresponding aldehydes (PubMed:28719588).
Catalyzes the reduction of a very wide range of carboxylic acids, including benzoic acids, heterocyclic, phenylacetic, phenylpropanoic and fatty acid substrates (PubMed:28719588).
Catalyzes the reduction of a very wide range of carboxylic acids, including benzoic acids, heterocyclic, phenylacetic, phenylpropanoic and fatty acid substrates (PubMed:28719588).
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 | 315 | AMP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 408 | AMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 429-430 | AMP (UniProtKB | ChEBI) | ||||
Sequence: DG | ||||||
Binding site | 434 | AMP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 507 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 519-522 | AMP (UniProtKB | ChEBI) | ||||
Sequence: YVDR | ||||||
Binding site | 528 | AMP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 629 | AMP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 801-804 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: NGWL | ||||||
Binding site | 828 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 838 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 868-869 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: DF | ||||||
Binding site | 894-896 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SGA | ||||||
Binding site | 934 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 970 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 974 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 997 | 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 | lipid 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
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Segniliparaceae > Segniliparus
Accessions
- Primary accessionE5XP76
Proteomes
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 900 | Loss of activity. | ||||
Sequence: H → P or N | ||||||
Mutagenesis | 966 | Loss of activity. | ||||
Sequence: Y → P | ||||||
Mutagenesis | 998 | Does not affect benzoic acid reduction rates but leads to alcohol production. Displays modest benzaldehyde reductase activity. | ||||
Sequence: D → G | ||||||
Mutagenesis | 1015 | Loss of activity. | ||||
Sequence: Q → P | ||||||
Mutagenesis | 1018 | Loss of activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 1131 | Loss of activity. | ||||
Sequence: L → Y |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000452836 | 1-1188 | Carboxylic acid reductase | |||
Sequence: MTESQSYETRQARPAGQSLAERVARLVAIDPQAAAAVPDKAVAERATQQGLRLAQRIEAFLSGYGDRPALAQRAFEITKDPITGRAVATLLPKFETVSYRELLERSHAIASELANHAEAPVKAGEFIATIGFTSTDYTSLDIAGVLLGLTSVPLQTGATTDTLKAIAEETAPAVFGASVEHLDNAVTTALATPSVRRLLVFDYRQGVDEDREAVEAARSRLAEAGSAVLVDTLDEVIARGRALPRVALPPATDAGDDSLSLLIYTSGSTGTPKGAMYPERNVAQFWGGIWHNAFDDGDSAPDVPDIMVNFMPLSHVAGRIGLMGTLSSGGTTYFIAKSDLSTFFEDYSLARPTKLFFVPRICEMIYQHYQSELDRIGAADGSPQAEAIKTELREKLLGGRVLTAGSGSAPMSPELTAFIESVLQVHLVDGYGSTEAGPVWRDRKLVKPPVTEHKLIDVPELGYFSTDSPYPRGELAIKTQTILPGYYKRPETTAEVFDEDGFYLTGDVVAEVAPEEFVYVDRRKNVLKLSQGEFVALSKLEAAYGTSPLVRQISVYGSSQRSYLLAVVVPTPEALAKYGDGEAVKSALGDSLQKIAREEGLQSYEVPRDFIIETDPFTIENGILSDAGKTLRPKVKARYGERLEALYAQLAETQAGELRSIRVGAGERPVIETVQRAAAALLGASAAEVDPEAHFSDLGGDSLSALTYSNFLHEIFQVEVPVSVIVSAANNLRSVAAHIEKERSSGSDRPTFASVHGAGATTIRASDLKLEKFLDAQTLAAAPSLPRPASEVRTVLLTGSNGWLGRFLALAWLERLVPQGGKVVVIVRGKDDKAAKARLDSVFESGDPALLAHYEDLADKGLEVLAGDFSDADLGLRKADWDRLADEVDLIVHSGALVNHVLPYSQLFGPNVVGTAEVAKLALTKRLKPVTYLSTVAVAVGVEPSAFEEDGDIRDVSAVRSIDEGYANGYGNSKWAGEVLLREAYEHAGLPVRVFRSDMILAHRKYTGQLNVPDQFTRLILSLLATGIAPKSFYQLDATGGRQRAHYDGIPVDFTAEAITTLGLAGSDGYHSFDVFNPHHDGVGLDEFVDWLVEAGHPISRVDDYAEWLSRFETSLRGLPEAQRQHSVLPLLHAFAQPAPAIDGSPFQTKNFQSSVQEAKVGAEHDIPHLDKALIVKYAEDIKQLGLL | ||||||
Modified residue | 702 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 665-743 | Carrier | ||||
Sequence: AGERPVIETVQRAAAALLGASAAEVDPEAHFSDLGGDSLSALTYSNFLHEIFQVEVPVSVIVSAANNLRSVAAHIEKER |
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 (By similarity).
Large-scale domain motions occur between the adenylation and thiolation states. Phosphopantetheine binding alters the orientation of a key Asp, resulting in a productive orientation of the bound nicotinamide. This ensures that further reduction of the aldehyde product does not occur (PubMed:28719588).
Large-scale domain motions occur between the adenylation and thiolation states. Phosphopantetheine binding alters the orientation of a key Asp, resulting in a productive orientation of the bound nicotinamide. This ensures that further reduction of the aldehyde product does not occur (PubMed:28719588).
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,188
- Mass (Da)128,228
- Last updated2011-03-08 v1
- Checksum6E86BB01FEAB63D8
Keywords
- Technical term