C6KEM4 · AADH2_MAIZE
- ProteinAminoaldehyde dehydrogenase 2
- GeneAMADH2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids506 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Dehydrogenase that catalyzes the oxidation of several aminoaldehydes (PubMed:23408433).
Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively (PubMed:23408433).
Catalyzes the oxidation of 4-(trimethylamino)butanal and 4-guanidinobutanal to 4-trimethylammoniobutanoate and 4-guanidinobutanoate, respectively (PubMed:23408433).
Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively (PubMed:23408433).
Catalyzes the oxidation of 4-(trimethylamino)butanal and 4-guanidinobutanal to 4-trimethylammoniobutanoate and 4-guanidinobutanoate, respectively (PubMed:23408433).
Catalytic activity
- 4-aminobutanal + H2O + NAD+ = 4-aminobutanoate + 2 H+ + NADHThis reaction proceeds in the forward direction.
- 3-aminopropanal + H2O + NAD+ = beta-alanine + 2 H+ + NADHThis reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
59 μM | 4-aminobutanal | |||||
98 μM | 3-aminopropanal | |||||
16 μM | 4-(trimethylamino)butanal | |||||
11 μM | 4-guanidinobutanal | |||||
86 μM | NAD+ with 3-aminopropanal as substrate |
Pathway
Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 101 | Na+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 161-163 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TPW | ||||||
Site | 164 | Transition state stabilizer | ||||
Sequence: N | ||||||
Binding site | 187-190 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: KPSE | ||||||
Binding site | 191 | Na+ (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 241-244 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: STET | ||||||
Active site | 262 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 262 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 297 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 396 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 462 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: W |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | peroxisome | |
Molecular Function | 4-trimethylammoniobutyraldehyde dehydrogenase activity | |
Molecular Function | aminobutyraldehyde dehydrogenase activity | |
Molecular Function | betaine-aldehyde dehydrogenase activity | |
Molecular Function | gamma-guanidinobutyraldehyde dehydrogenase activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | sodium ion binding | |
Biological Process | cellular detoxification of aldehyde | |
Biological Process | cellular response to anoxia | |
Biological Process | glycine betaine biosynthetic process from choline |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAminoaldehyde dehydrogenase 2
- EC number
- Short namesZmAMADH2
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Andropogonodae > Andropogoneae > Tripsacinae > Zea
Accessions
- Primary accessionC6KEM4
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000454137 | 1-506 | Aminoaldehyde dehydrogenase 2 | |||
Sequence: MAPPQTIPRRGLFIGGAWREPCLGRRLPVVNPATEATIGDIPAGTAEDVEIAVAAARDAFSRDGGRHWSRAPGAVRANFLRAIAAKIKDRKSELALLETLDSGKPLDEASGDMDDVAACFEYYADLAEALDGKQQSPISLPMENFKSYVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCTTILKPSELASVSCLELGAICMEIGLPPGVLNIITGLGPEAGAPLSSHSHVDKVAFTGSTETGKRIMISAAQMVKPVSLELGGKSPLIVFDDIGDIDKAVEWTMFGIFANAGQVCSATSRLLLHEKIAKKFLDRLVAWAKNIKVSDPLEEGCRLGSVISEGQYEKIKKFISTARSEGATILYGGGRPQHLRRGFFLEPTIITDVSTSMQIWQEEVFGPVICVKEFRTESEAVELANDTHYGLAGAVISNDQERCERISKALHSGIIWINCSQPCFVQAPWGGNKRSGFGRELGEWGLDNYLTVKQVTKYCSDEPWGWYQPPSKL |
Proteomic databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length506
- Mass (Da)54,862
- Last updated2022-02-23 v2
- Checksum8033CB10EF67B5A3
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 67 | in Ref. 1; ACS74868 | ||||
Sequence: H → Q | ||||||
Sequence conflict | 135 | in Ref. 1; ACS74868 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 202 | in Ref. 3; ACG29220 | ||||
Sequence: I → T | ||||||
Sequence conflict | 250 | in Ref. 1; ACS74868 and 3; ACG29220 | ||||
Sequence: I → T | ||||||
Sequence conflict | 274 | in Ref. 3; ACG29220 | ||||
Sequence: D → G | ||||||
Sequence conflict | 410 | in Ref. 1; ACS74868 | ||||
Sequence: E → D | ||||||
Sequence conflict | 442 | in Ref. 3; ACG29220 | ||||
Sequence: A → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GQ184594 EMBL· GenBank· DDBJ | ACS74868.1 EMBL· GenBank· DDBJ | mRNA | ||
CM000786 EMBL· GenBank· DDBJ | AQK44108.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CM000786 EMBL· GenBank· DDBJ | AQK44109.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
EU957102 EMBL· GenBank· DDBJ | ACG29220.1 EMBL· GenBank· DDBJ | mRNA | ||
BT042732 EMBL· GenBank· DDBJ | ACF87737.1 EMBL· GenBank· DDBJ | mRNA | ||
BT067636 EMBL· GenBank· DDBJ | ACN34533.1 EMBL· GenBank· DDBJ | mRNA |