Q1RFI7 · FRMA_ECOUT

Function

function

Has high formaldehyde dehydrogenase activity in the presence of glutathione and catalyzes the oxidation of normal alcohols in a reaction that is not GSH-dependent. In addition, hemithiolacetals other than those formed from GSH, including omega-thiol fatty acids, also are substrates. Also acts as a S-nitroso-glutathione reductase by catalyzing the NADH-dependent reduction of S-nitrosoglutathione.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site40Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site62Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site92Zn2+ 2 (UniProtKB | ChEBI)
Binding site95Zn2+ 2 (UniProtKB | ChEBI)
Binding site98Zn2+ 2 (UniProtKB | ChEBI)
Binding site106Zn2+ 2 (UniProtKB | ChEBI)
Binding site169Zn2+ 1 (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionalcohol dehydrogenase (NAD+) activity
Molecular FunctionS-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity
Molecular FunctionS-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity
Molecular Functionzinc ion binding
Biological Processformaldehyde catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    S-(hydroxymethyl)glutathione dehydrogenase
  • EC number
  • Alternative names
    • Alcohol dehydrogenase class-3 (EC:1.1.1.1) . EC:1.1.1.1 (UniProtKB | ENZYME | Rhea)
    • Alcohol dehydrogenase class-III
    • Glutathione-dependent formaldehyde dehydrogenase (FALDH; FDH; GSH-FDH) (EC:1.1.1.-) . EC:1.1.1.- (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      frmA
    • Ordered locus names
      UTI89_C0376

Organism names

Accessions

  • Primary accession
    Q1RFI7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003412851-369S-(hydroxymethyl)glutathione dehydrogenase

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    369
  • Mass (Da)
    39,347
  • Last updated
    2006-05-16 v1
  • Checksum
    760D615FF801ED20
MKSRAAVAFAPGKPLEIVEIDVAPPKKGEVLIKVTHTGVCHTDAFTLSGDDPEGVFPVVLGHEGAGVVVEVGEGVTSVKPGDHVIPLYTAECGECEFCRSGKTNLCVAVRETQGKGLMPDGTTRFSYNGQPLYHYMGCSTFSEYTVVAEVSLAKINPEANHEHVCLLGCGVTTGIGAVHNTAKVQPGDSVAVFGLGAIGLAVVQGARQAKAGRIIAIDTNPKKFELARRFGATDCINPNDYDKPIKDVLLDINKWGIDHTFECIGNVNVMRAALESAHRGWGQSVIIGVAGSGQEISTRPFQLVTGRVWKGSAFGGVKGRSQLPGMVEDAMKGDIDLEPFVTHTMSLDEINDAFDLMHEGKSIRTVIRY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000243
EMBL· GenBank· DDBJ
ABE05877.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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