Q8R0Y6 · AL1L1_MOUSE

  • Protein
    Cytosolic 10-formyltetrahydrofolate dehydrogenase
  • Gene
    Aldh1l1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Cytosolic 10-formyltetrahydrofolate dehydrogenase that catalyzes the NADP+-dependent conversion of 10-formyltetrahydrofolate to tetrahydrofolate and carbon dioxide (PubMed:31624291).
May also have an NADP+-dependent aldehyde dehydrogenase activity towards formaldehyde, acetaldehyde, propionaldehyde, and benzaldehyde (By similarity).

Catalytic activity

Features

Showing features for binding site, active site, site.

1902100200300400500600700800900
TypeIDPosition(s)Description
Binding site88-90(6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI)
Active site106Proton donor
Binding site142(6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI)
Site142Essential for catalytic activity
Binding site571-573NADP+ (UniProtKB | ChEBI)
Binding site597-600NADP+ (UniProtKB | ChEBI)
Binding site630-635NADP+ (UniProtKB | ChEBI)
Binding site650-651NADP+ (UniProtKB | ChEBI)
Active site673Proton acceptor
Binding site673-674NADP+ (UniProtKB | ChEBI)
Active site707Proton donor
Binding site757NADP+ (UniProtKB | ChEBI)
Binding site804-806NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmitochondrion
Cellular Componentprotein-containing complex
Molecular Functionaldehyde dehydrogenase (NAD+) activity
Molecular Functionaldehyde dehydrogenase (NADP+) activity
Molecular Functionaldehyde dehydrogenase [NAD(P)+] activity
Molecular Functionformyltetrahydrofolate dehydrogenase activity
Molecular Functionprotein-containing complex binding
Biological Process10-formyltetrahydrofolate catabolic process
Biological Processbiosynthetic process
Biological Processfolic acid metabolic process
Biological ProcessNADPH regeneration
Biological Processone-carbon metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytosolic 10-formyltetrahydrofolate dehydrogenase
  • EC number
  • Short names
    10-FTHFDH; FDH
  • Alternative names
    • Aldehyde dehydrogenase family 1 member L1

Gene names

    • Name
      Aldh1l1
    • Synonyms
      Fthfd

Organism names

  • Taxonomic identifier
  • Strain
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8R0Y6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Homozygous knockout mice are viable, fertile, develop normally and do not display overt phenotype (PubMed:31624291).
However, they have metabolic signs of folate deficiency like the accumulation of formiminoglutamate (PubMed:31624291).
Mice show reduced hepatic folate pools with a strong accumulation of (6S)-10-formyltetrahydrofolate and a significant drop in tetrahydrofolate levels (PubMed:31624291).
This is associated with a strong decrease of glycine levels as well as levels of several glycine conjugates (PubMed:31624291).

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 61 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001994201-902Cytosolic 10-formyltetrahydrofolate dehydrogenase
Modified residue9Phosphoserine
Modified residue38N6-succinyllysine
Modified residue354O-(pantetheine 4'-phosphoryl)serine
Modified residue629Phosphoserine
Modified residue631Phosphoserine
Modified residue660N6-succinyllysine
Modified residue767N6-succinyllysine
Modified residue825Phosphoserine
Modified residue882N6-acetyllysine

Post-translational modification

Phosphopantetheinylation at Ser-354 by AASDHPPT is required for the formyltetrahydrofolate dehydrogenase activity.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Highly expressed in liver (at protein level) (PubMed:31624291).
Also expressed in pancreas, brain and lung (at protein level) (PubMed:31624291).

Gene expression databases

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-310Hydrolase domain
Domain318-395Carrier
Region417-902Aldehyde dehydrogenase domain

Domain

The N-terminal hydrolase domain has an NADP-independent formyltetrahydrofolate hydrolase activity, releasing formate and tetrahydrofolate.
The C-terminal aldehyde dehydrogenase domain has an NADP-dependent dehydrogenase activity. It catalyzes the oxidation of formate, released by the hydrolysis of formyltetrahydrofolate, into CO2.
The carrier domain is phosphopantetheinylated and uses the 4'-phosphopantetheine/4'-PP swinging arm to transfer the formyl group released by the N-terminal formyltetrahydrofolate hydrolase activity to the C-terminal aldehyde dehydrogenase domain that catalyzes its NADP-dependent oxidation into CO2. The overall NADP-dependent physiological reaction requires the 3 domains (N-terminal hydrolase, C-terminal aldehyde dehydrogenase and carrier domains) to convert formyltetrahydrofolate into tetrahydrofolate and CO2.

Sequence similarities

In the N-terminal section; belongs to the GART family.
In the C-terminal section; belongs to the aldehyde dehydrogenase family. ALDH1L subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    902
  • Mass (Da)
    98,709
  • Last updated
    2002-06-01 v1
  • Checksum
    9B5526A7FB41909E
MKIAVIGQSLFGQEVYCQLRKEGHEVVGVFTIPDKDGKADPLGLEAEKDGVPVFKFPRWRARGQALPEVVAKYQALGAELNVLPFCSQFIPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDVLPDDTVSTLYNRFLFPEGIKGMVQAVRLIAEGTAPRRPQPEEGATYEGIQKKETAMINWDQPAEAIHNWIRGNDKVPGAWTEACGQKLTFFNSTLNTSGLVAQGEALPIPGAHRPGLVTKAGLILFGNDDRMLLVKNIQLEDGKMMPASQFFKGSASSALELTEEELATAEAVRSSWMRILPNVPEVEDSTDFFKSGAASVDVVRLVEEVKELCDGLELENEDVYMATTFGDFIQLLVRKLRGEDGESECVINYVEKAVKKLTLQMPYQLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINQARPNRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCALSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTFEY

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0N4SVT2A0A0N4SVT2_MOUSEAldh1l1135
A0A0N4SW56A0A0N4SW56_MOUSEAldh1l1359

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC025939
EMBL· GenBank· DDBJ
AAH25939.1
EMBL· GenBank· DDBJ
mRNA
BC028817
EMBL· GenBank· DDBJ
AAH28817.1
EMBL· GenBank· DDBJ
mRNA
BC030722
EMBL· GenBank· DDBJ
AAH30722.1
EMBL· GenBank· DDBJ
mRNA
BC030723
EMBL· GenBank· DDBJ
AAH30723.1
EMBL· GenBank· DDBJ
mRNA
BC030727
EMBL· GenBank· DDBJ
AAH30727.1
EMBL· GenBank· DDBJ
mRNA
BC030730
EMBL· GenBank· DDBJ
AAH30730.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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