O75891 · AL1L1_HUMAN
- ProteinCytosolic 10-formyltetrahydrofolate dehydrogenase
- GeneALDH1L1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids902 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May also have an NADP+-dependent aldehyde dehydrogenase activity towards formaldehyde, acetaldehyde, propionaldehyde, and benzaldehyde (By similarity).
Catalytic activity
- (6R)-10-formyltetrahydrofolate + H2O + NADP+ = (6S)-5,6,7,8-tetrahydrofolate + CO2 + H+ + NADPHThis reaction proceeds in the forward direction.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 88-90 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: QFI | ||||||
Active site | 106 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 142 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 142 | Essential for catalytic activity | ||||
Sequence: D | ||||||
Binding site | 571-573 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: IPW | ||||||
Binding site | 597-600 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: KPAQ | ||||||
Binding site | 630-635 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GSLVGQ | ||||||
Binding site | 650-651 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GS | ||||||
Active site | 673 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 673-674 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: EL | ||||||
Active site | 707 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 757 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 804-806 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: ESF |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Molecular Function | aldehyde dehydrogenase (NAD+) activity | |
Molecular Function | formyltetrahydrofolate dehydrogenase activity | |
Biological Process | 10-formyltetrahydrofolate catabolic process | |
Biological Process | biosynthetic process | |
Biological Process | NADPH regeneration | |
Biological Process | one-carbon metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytosolic 10-formyltetrahydrofolate dehydrogenase
- EC number
- Short names10-FTHFDH; FDH
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO75891
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_052290 | 254 | in dbSNP:rs3796191 | |||
Sequence: L → P | ||||||
Natural variant | VAR_052291 | 330 | in dbSNP:rs2886059 | |||
Sequence: V → F | ||||||
Mutagenesis | 354 | Loss of phosphopantetheinylation by AASDHPPT. Loss of formyltetrahydrofolate dehydrogenase activity. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_052292 | 429 | in dbSNP:rs9282691 | |||
Sequence: E → A | ||||||
Natural variant | VAR_052293 | 436 | in dbSNP:rs9282692 | |||
Sequence: A → T | ||||||
Natural variant | VAR_052295 | 448 | in dbSNP:rs9282697 | |||
Sequence: S → N | ||||||
Natural variant | VAR_052296 | 481 | in dbSNP:rs2276724 | |||
Sequence: S → G | ||||||
Natural variant | VAR_036101 | 511 | in a colorectal cancer sample; somatic mutation; dbSNP:rs768309358 | |||
Sequence: A → V | ||||||
Natural variant | VAR_052297 | 793 | in dbSNP:rs1127717 | |||
Sequence: D → G | ||||||
Natural variant | VAR_052298 | 803 | in dbSNP:rs9282689 | |||
Sequence: E → K | ||||||
Natural variant | VAR_052299 | 812 | in dbSNP:rs4646750 | |||
Sequence: I → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,230 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000199419 | 1-902 | UniProt | Cytosolic 10-formyltetrahydrofolate dehydrogenase | |||
Sequence: MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGDALPIPGAHRPGVVTKAGLILFGNDDKMLLVKNIQLEDGKMILASNFFKGAASSVLELTEAELVTAEAVRSVWQRILPKVLEVEDSTDFFKSGAASVDVVRLVEEVKELCDGLELENEDVYMASTFGDFIQLLVRKLRGDDEEGECSIDYVEMAVNKRTVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTFEY | |||||||
Modified residue | 9 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 38 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 354 | UniProt | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S | |||||||
Modified residue | 629 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 629 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 631 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 660 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 767 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 825 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 882 | UniProt | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O75891 | ALDH1L2 Q3SY69 | 2 | EBI-10714847, EBI-6916128 | |
BINARY | O75891-4 | APPBP2 Q92624 | 3 | EBI-12400198, EBI-743771 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-310 | Hydrolase domain | ||||
Sequence: MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGDALPIPGAHRPGVVTKAGLILFGNDDKMLLVKNIQLEDGKMILASNFFKGAA | ||||||
Domain | 318-395 | Carrier | ||||
Sequence: EAELVTAEAVRSVWQRILPKVLEVEDSTDFFKSGAASVDVVRLVEEVKELCDGLELENEDVYMASTFGDFIQLLVRKL | ||||||
Region | 417-902 | Aldehyde dehydrogenase domain | ||||
Sequence: TVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTFEY |
Domain
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
O75891-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length902
- Mass (Da)98,829
- Last updated2005-02-15 v2
- ChecksumD92CB2930617F7CF
O75891-2
- Name2
- Differences from canonical
- 118-218: Missing
O75891-3
- Name3
- Differences from canonical
- 1-1: M → MAGPSNPPATM
O75891-4
- Name4
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_047260 | 1 | in isoform 3 | |||
Sequence: M → MAGPSNPPATM | ||||||
Sequence conflict | 63 | in Ref. 1; AAC35000 | ||||
Sequence: G → A | ||||||
Sequence conflict | 85 | in Ref. 1; AAC35000 | ||||
Sequence: F → S | ||||||
Alternative sequence | VSP_045569 | 118-218 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 176 | in Ref. 1; AAC35000 | ||||
Sequence: M → V | ||||||
Sequence conflict | 195 | in Ref. 1; AAC35000 | ||||
Sequence: E → K | ||||||
Sequence conflict | 470 | in Ref. 1; AAC35000 | ||||
Sequence: D → G | ||||||
Sequence conflict | 472 | in Ref. 2; BAG57647 | ||||
Sequence: F → L | ||||||
Alternative sequence | VSP_057429 | 492-505 | in isoform 4 | |||
Sequence: LADLMEQHQEELAT → APPSPSTRPDPTAT | ||||||
Alternative sequence | VSP_057430 | 506-902 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 677 | in Ref. 1; AAC35000 | ||||
Sequence: K → E | ||||||
Sequence conflict | 680 | in Ref. 1; AAC35000 | ||||
Sequence: L → F | ||||||
Sequence conflict | 702 | in Ref. 1; AAC35000 | ||||
Sequence: N → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF052732 EMBL· GenBank· DDBJ | AAC35000.1 EMBL· GenBank· DDBJ | mRNA | ||
AK294392 EMBL· GenBank· DDBJ | BAG57647.1 EMBL· GenBank· DDBJ | mRNA | ||
CR749807 EMBL· GenBank· DDBJ | CAH18667.1 EMBL· GenBank· DDBJ | mRNA | ||
AC079848 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471052 EMBL· GenBank· DDBJ | EAW79370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC027241 EMBL· GenBank· DDBJ | AAH27241.1 EMBL· GenBank· DDBJ | mRNA |