E5XP76 · CAR_SEGRC

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).

Catalytic activity

Cofactor

pantetheine 4'-phosphate (UniProtKB | Rhea| CHEBI:47942 )

Note: Binds 1 phosphopantetheine covalently.

Features

Showing features for binding site.

111881002003004005006007008009001,0001,100
TypeIDPosition(s)Description
Binding site315AMP (UniProtKB | ChEBI)
Binding site408AMP (UniProtKB | ChEBI)
Binding site429-430AMP (UniProtKB | ChEBI)
Binding site434AMP (UniProtKB | ChEBI)
Binding site507AMP (UniProtKB | ChEBI)
Binding site519-522AMP (UniProtKB | ChEBI)
Binding site528AMP (UniProtKB | ChEBI)
Binding site629AMP (UniProtKB | ChEBI)
Binding site801-804NADP+ (UniProtKB | ChEBI)
Binding site828NADP+ (UniProtKB | ChEBI)
Binding site838NADP+ (UniProtKB | ChEBI)
Binding site868-869NADP+ (UniProtKB | ChEBI)
Binding site894-896NADP+ (UniProtKB | ChEBI)
Binding site934NADP+ (UniProtKB | ChEBI)
Binding site970NADP+ (UniProtKB | ChEBI)
Binding site974NADP+ (UniProtKB | ChEBI)
Binding site997NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionNADP binding
Molecular Functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Molecular Functionphosphopantetheine binding
Biological Processlipid metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Carboxylic acid reductase
  • EC number
  • Short names
    CAR
  • Alternative names
    • ATP/NADPH-dependent carboxylic acid reductase

Gene names

    • Name
      car
    • ORF names
      HMPREF9336_01297

Organism names

Accessions

  • Primary accession
    E5XP76

Proteomes

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis900Loss of activity.
Mutagenesis966Loss of activity.
Mutagenesis998Does not affect benzoic acid reduction rates but leads to alcohol production. Displays modest benzaldehyde reductase activity.
Mutagenesis1015Loss of activity.
Mutagenesis1018Loss of activity.
Mutagenesis1131Loss of activity.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004528361-1188Carboxylic acid reductase
Modified residue702O-(pantetheine 4'-phosphoryl)serine

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain665-743Carrier

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).

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,188
  • Mass (Da)
    128,228
  • Last updated
    2011-03-08 v1
  • Checksum
    6E86BB01FEAB63D8
MTESQSYETRQARPAGQSLAERVARLVAIDPQAAAAVPDKAVAERATQQGLRLAQRIEAFLSGYGDRPALAQRAFEITKDPITGRAVATLLPKFETVSYRELLERSHAIASELANHAEAPVKAGEFIATIGFTSTDYTSLDIAGVLLGLTSVPLQTGATTDTLKAIAEETAPAVFGASVEHLDNAVTTALATPSVRRLLVFDYRQGVDEDREAVEAARSRLAEAGSAVLVDTLDEVIARGRALPRVALPPATDAGDDSLSLLIYTSGSTGTPKGAMYPERNVAQFWGGIWHNAFDDGDSAPDVPDIMVNFMPLSHVAGRIGLMGTLSSGGTTYFIAKSDLSTFFEDYSLARPTKLFFVPRICEMIYQHYQSELDRIGAADGSPQAEAIKTELREKLLGGRVLTAGSGSAPMSPELTAFIESVLQVHLVDGYGSTEAGPVWRDRKLVKPPVTEHKLIDVPELGYFSTDSPYPRGELAIKTQTILPGYYKRPETTAEVFDEDGFYLTGDVVAEVAPEEFVYVDRRKNVLKLSQGEFVALSKLEAAYGTSPLVRQISVYGSSQRSYLLAVVVPTPEALAKYGDGEAVKSALGDSLQKIAREEGLQSYEVPRDFIIETDPFTIENGILSDAGKTLRPKVKARYGERLEALYAQLAETQAGELRSIRVGAGERPVIETVQRAAAALLGASAAEVDPEAHFSDLGGDSLSALTYSNFLHEIFQVEVPVSVIVSAANNLRSVAAHIEKERSSGSDRPTFASVHGAGATTIRASDLKLEKFLDAQTLAAAPSLPRPASEVRTVLLTGSNGWLGRFLALAWLERLVPQGGKVVVIVRGKDDKAAKARLDSVFESGDPALLAHYEDLADKGLEVLAGDFSDADLGLRKADWDRLADEVDLIVHSGALVNHVLPYSQLFGPNVVGTAEVAKLALTKRLKPVTYLSTVAVAVGVEPSAFEEDGDIRDVSAVRSIDEGYANGYGNSKWAGEVLLREAYEHAGLPVRVFRSDMILAHRKYTGQLNVPDQFTRLILSLLATGIAPKSFYQLDATGGRQRAHYDGIPVDFTAEAITTLGLAGSDGYHSFDVFNPHHDGVGLDEFVDWLVEAGHPISRVDDYAEWLSRFETSLRGLPEAQRQHSVLPLLHAFAQPAPAIDGSPFQTKNFQSSVQEAKVGAEHDIPHLDKALIVKYAEDIKQLGLL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ACZI02000003
EMBL· GenBank· DDBJ
EFV13858.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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