Q7YS70 · MECR_BOVIN

  • Protein
    Enoyl-[acyl-carrier-protein] reductase, mitochondrial
  • Gene
    MECR
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II) (PubMed:12654921).
Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Displays a preference for medium-chain over short- and long-chain substrates (By similarity).
May provide the octanoyl chain used for lipoic acid biosynthesis, regulating protein lipoylation and mitochondrial respiratory activity particularly in Purkinje cells (By similarity).
Involved in iron homeostasis; affecting Fe-S cluster assembly and ceramide metabolism (By similarity).
Required for proper morphology and bioenergetic functions of mitochondria (By similarity).
Required for maintenance of neurons (By similarity).

Catalytic activity

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site94Proton donor
Binding site167NADP+ (UniProtKB | ChEBI)
Binding site193-196NADP+ (UniProtKB | ChEBI)
Binding site216-218NADP+ (UniProtKB | ChEBI)
Binding site285-288NADP+ (UniProtKB | ChEBI)
Binding site310-312NADP+ (UniProtKB | ChEBI)
Binding site368NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrion
Molecular Functionenoyl-[acyl-carrier-protein] reductase (NADPH) activity
Biological Processceramide biosynthetic process
Biological Processfatty acid biosynthetic process
Biological Processfatty acid metabolic process
Biological Processintracellular iron ion homeostasis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Enoyl-[acyl-carrier-protein] reductase, mitochondrial
  • EC number
  • Alternative names
    • 2-enoyl thioester reductase
    • Nuclear receptor-binding factor 1 (BtNrbf-1; NRBF-1)

Gene names

    • Name
      MECR
    • Synonyms
      NBRF1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    Q7YS70

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain, modified residue.

TypeIDPosition(s)Description
Transit peptide1-53Mitochondrion
ChainPRO_000000088754-373Enoyl-[acyl-carrier-protein] reductase, mitochondrial
Modified residue61N6-acetyllysine; alternate
Modified residue61N6-succinyllysine; alternate
Modified residue252N6-acetyllysine; alternate
Modified residue252N6-succinyllysine; alternate
Modified residue267N6-acetyllysine; alternate
Modified residue267N6-succinyllysine; alternate
Modified residue316N6-succinyllysine

Keywords

Proteomic databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    373
  • Mass (Da)
    40,275
  • Last updated
    2003-10-01 v1
  • Checksum
    7921122C7735A95D
MWVCGALCRTRAPAQLGQRLLPESRRRRPASASFSASAEPSRVRALVYGHHGDPAKVVELKNLELAAVGGSHVHVKMLAAPINPSDINMIQGNYGLLPQLPAVGGNEGVGQVVAVGSGVTGVKPGDWVIPANPGLGTWRTEAVFGEEELITVPSDIPLQSAATLGVNPCTAYRMLVDFERLRPRDSIIQNASNSGVGQAVIQIAAARGLRTINVLRDTPDLQKLTDTLKNLGANHVVTEEELRKPEMKSFFKDVPQPRLALNCVGGKSSTELLRHLAPGGTMVTYGGMAKQPVIASVSQLIFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSEVPLQDYLCALEASTQPFVSSKQILTM

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY256973
EMBL· GenBank· DDBJ
AAP45003.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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