B1VMZ4 · B1VMZ4_STRGG

Function

function

Catalyzes the ATP- and NADPH-dependent reduction of carboxylic acids to the corresponding aldehydes.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

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

Note: Binds 1 phosphopantetheine covalently.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site276AMP (UniProtKB | ChEBI)
Binding site368AMP (UniProtKB | ChEBI)
Binding site394AMP (UniProtKB | ChEBI)
Binding site467AMP (UniProtKB | ChEBI)
Binding site479-482AMP (UniProtKB | ChEBI)
Binding site488AMP (UniProtKB | ChEBI)
Binding site590AMP (UniProtKB | ChEBI)
Binding site763-766NADP+ (UniProtKB | ChEBI)
Binding site790NADP+ (UniProtKB | ChEBI)
Binding site800NADP+ (UniProtKB | ChEBI)
Binding site856-858NADP+ (UniProtKB | ChEBI)
Binding site896NADP+ (UniProtKB | ChEBI)
Binding site932NADP+ (UniProtKB | ChEBI)
Binding site936NADP+ (UniProtKB | ChEBI)
Binding site959NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmembrane
Molecular FunctionATP binding
Molecular Functionlong-chain fatty acid-CoA ligase activity
Molecular FunctionNADP binding
Molecular Functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Molecular Functionphosphopantetheine binding
Biological Processantibiotic biosynthetic 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
    • Ordered locus names
      SGR_6790

Organism names

Accessions

  • Primary accession
    B1VMZ4

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue663O-(pantetheine 4'-phosphoryl)serine

Keywords

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain629-704Carrier

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 status
    Complete
  • Length
    1,148
  • Mass (Da)
    123,158
  • Last updated
    2008-05-20 v1
  • MD5 Checksum
    7E247579D5B9A0A7480C26ED9AB6E4CC
MAEPLDAATASAHDPGQGLAEALAAVEPGRALAEVMASVLEGHGDRPALGERAREPETGRLLPHFDTISYRELWSRVRALAGRWHHDPEYPLGPGDRICTLGFTSTDYATLDLACIHLGAVPVPLPSNAPLPRLAPVVEESGPTVLAASVDRLDTAIDVVLASSTIRRLLVFDDGPGATRPGGALAAARQRLSGSPVTVDTLAGLIDRGRDLPPPPLYIPDPGEDPLALLIYTSGSTGAPKGAMYTQRLLGTAWYGFSYGAADTPAISVLYLPQSHLAGRYAVMGSLVKGGTGYFTAADDLSTLFEDIALVRPTELTMVPRLCDMLLQHYRSERDRRADEPGDIEAAVTKAVREDFLGGRVAKAFVGTAPLSAELTAFVESVLGFHLYTGYGSTEAGGVLLDTVVQRPPVTDYKLVDVPELGYYATDLPHPRGELLLKSHTLIPGYYRRPDLTAAIFDADGYYRTGDVFAETGPDRLVYVDRTKDTLKLSQGEFVAVSRLETVLLDSPLVQHLYLYGNSERAYLLAVVVPTPDALAGCGGDTEALRPLLMESLRSVARRAGLNAYEIPRGILVEPEPFSPENGLFTESHKLLRPRLKERYGPALELLYDRLADGQDRRLRELRRTGADRPVQETVLRAAQALLGSPGSDLRPGAHFTDLGGDSLSAVSFSELMKEIFHVDVPVGAIIGPAADLAEVARYITAARRPAGAPRPTPASVHGEHRTEVRAGDLAPEKFLDAPTLAAAPALPRPDGDVRTVLLTGATGYLGRFLCLEWLERLAPSGGRLVCLVRGSDATVAARRLEAAFDSGDTALLRRYRKAAGKTLDVVAGDIGEPLLGLAEETWRELAGAVDLIVHPAALVNHLLPYGELFGPNVVGTAEAIRLALTTRLKPVNHVSTVAVCLGTPAETADENADIRAAVPVRTTGQGYADGYATSKWAGEVLLREAHERYGLPVAVFRSDMVLAHRTYTGQVNVPDVLTRLLLSLVATGIAPGSFYRTDTRAHYDGLPVDFTAEAVVALGAPITEGHRTFNVLNPHDDGVSLDTFVDWLIEAGHPIRRIDDHGAWLTRFTAALRALPEKQRQHSLLPLIGAWAEPGEGAPGPLLPARRFHAAVRAAGVGPERDIPRVSPDLIRKYVTDLRALGLLAGP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP009493
EMBL· GenBank· DDBJ
BAG23619.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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