Q6GNL7 · AL1L1_XENLA

Function

function

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

Catalytic activity

Features

Showing features for binding site, active site, site.

1902100200300400500600700800900
Type
IDPosition(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
Molecular Functionaldehyde dehydrogenase (NAD+) activity
Molecular Functionformyltetrahydrofolate dehydrogenase activity
Biological Process10-formyltetrahydrofolate catabolic process
Biological Processbiosynthetic 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

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus

Accessions

  • Primary accession
    Q6GNL7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00003159991-902Cytosolic 10-formyltetrahydrofolate dehydrogenase
Modified residue354O-(pantetheine 4'-phosphoryl)serine

Post-translational modification

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

Keywords

Expression

Gene expression databases

    • 444321Expressed in kidney and 15 other cell types or tissues

Interaction

Subunit

Homotetramer.

Structure

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(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)
    99,982
  • Last updated
    2004-07-19 v1
  • Checksum
    C484728096D4C281
MKIAVIGQSLFGREVYRELLKEGHQVVGVFTIPDKNGKADPLGADAEKDGIPVFKFPRWRVKGQAIPEVVEKYKALEAELNVLPFCSQFIPMEVIDCPKHGSIIYHPSILPRHRGASAINWTLMQGDKIGGFTVFWADDGLDTGDILLQRQCEVLPDDTVNTIYNRFLFPEGVKGMVEAVRLIAEGNAPRIKQPTEGATYDPMQKKENAKINWDQPAEDIHNFIRGNDKVPGAWTVVDDQQLTFFGSSFTRNGPAPDGQPLEIPGASRPALVTKTGLVLFGNDGERLTVKNIQFEDGKMIPASQYFKTADSAALQLSEEEQKVSEEIRAAWRRILTNVSEIEDSTDFFKAGAASMDVVRLVEEVKLKCNGLQLQNEDVYMATKFEEFIQMVVRRMRGEDGEEELVIDYVEKEINNMTVKIPHQLFINGQFMDAEGGKSYDTINPTDGTAICKVSLAQISDIDRAVAAAKEAFENGEWGKMNPRDRGRLLYRLADLMEEHQEELATIESIDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGRTIPINQARPNRNLTFTRREPIGVCGIVIPWNYPLMMLAWKTAACLTAGNTVVLKPAQVTPLTALKFAELSVKAGIPKGVINILPGAGSLIGQRLSDHPDVRKIGFTGSTPIGKQIMKSCAVSNVKKVSLELGGKSPLIIFHDCDLDKAVRMGMSSVFFNKGENCIAAGRLFLEESIHDEFVKRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLIEYCQTGVKEGGKLVYGGKQVERPGFFFEPTIFTDVTDEMFIAKEESFGPVMIISKFNDGDIDGVLKRANDSEFGLASGVFTKDINKALYVSEKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKAVTIEY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC073490
EMBL· GenBank· DDBJ
AAH73490.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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