Q0PGJ6 · AKRC9_ARATH
- ProteinNADPH-dependent aldo-keto reductase, chloroplastic
- GeneAKR4C9
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids315 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Oxidoreductase acting on a broad range of substrates: reduces ketosteroids, aromatic aldehydes, ketones, sugars and other aliphatic aldehydes, and oxidizes hydroxysteroids (PubMed:19616008).
Aldehyde reductase that catalyzes the reduction of the aldehyde carbonyl groups on saturated and alpha,beta-unsaturated aldehydes (PubMed:21169366).
No activity on alpha,beta-unsaturated ketones (PubMed:21169366).
Can use propionaldehyde, butyraldehyde, methylglyoxal, (E)-2-pentenal, (E)-2-hexenal, (Z)-3-hexenal and (E)-2-nonenal as substrates, propenal (acrolein), crotonaldehyde, but not 2-butanone, 3-buten-2-one or 1-penten-3-one (PubMed:21169366).
May function as detoxifiying enzyme by reducing a range of toxic aldehydes and ketones produced during stress (PubMed:19616008).
Aldehyde reductase that catalyzes the reduction of the aldehyde carbonyl groups on saturated and alpha,beta-unsaturated aldehydes (PubMed:21169366).
No activity on alpha,beta-unsaturated ketones (PubMed:21169366).
Can use propionaldehyde, butyraldehyde, methylglyoxal, (E)-2-pentenal, (E)-2-hexenal, (Z)-3-hexenal and (E)-2-nonenal as substrates, propenal (acrolein), crotonaldehyde, but not 2-butanone, 3-buten-2-one or 1-penten-3-one (PubMed:21169366).
May function as detoxifiying enzyme by reducing a range of toxic aldehydes and ketones produced during stress (PubMed:19616008).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1445 μM | benzaldehyde | |||||
102 μM | 3-fluorobenzaldehyde | |||||
270 μM | cinnamylaldehyde | |||||
261 μM | 3-hydroxybenzaldehyde | |||||
82 μM | isopropylbenzaldehyde | |||||
4.4 μM | 9,10-phenanthrenequinone | |||||
5.49 mM | 2-E-hexenal | |||||
4 mM | 4-hydroxy-2-nonenal | |||||
51 mM | malondialdehyde | |||||
0.46 mM | methylglyoxal | |||||
2.2 mM | glyceraldehyde | |||||
10.2 mM | glyoxal | |||||
2.8 mM | erythrose | |||||
238 mM | xylose | |||||
240 mM | arabinose | |||||
760 mM | glucose | |||||
121 mM | galactose | |||||
70 mM | propionaldehyde | |||||
6.9 mM | butyraldehyde | |||||
2.6 mM | acrolein | |||||
1.63 mM | crotonaldehyde | |||||
0.63 mM | (E)-2-pentenal | |||||
0.72 mM | (E)-2-hexenal | |||||
1.67 mM | (E)-2-nonenal | |||||
0.24 mM | methylglyoxal |
kcat is 44 sec-1 for propionaldehyde. kcat is 21 sec-1 for butyraldehyde. kcat is 6.6 sec-1 for acrolein. kcat is 18 sec-1 for crotonaldehyde. kcat is 9.5 sec-1 for (E)-2-pentenal. kcat is 7.3 sec-1 for (E)-2-hexenal. kcat is 7.9 sec-1 for (E)-2-nonenal. kcat is 11.5 sec-1 for methylglyoxal.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 23-24 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: TW | ||||||
Binding site | 47 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 52 | Proton donor | ||||
Sequence: Y | ||||||
Binding site | 114 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 158-159 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SN | ||||||
Binding site | 180 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 207-213 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SPLGSPG | ||||||
Binding site | 256-258 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: KST | ||||||
Binding site | 262-266 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: RIKEN |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | endoplasmic reticulum | |
Molecular Function | alcohol dehydrogenase (NADP+) activity | |
Molecular Function | aldo-keto reductase (NADPH) activity | |
Molecular Function | NADP+ binding | |
Molecular Function | steroid dehydrogenase activity | |
Biological Process | response to cold | |
Biological Process | response to salt stress | |
Biological Process | response to toxic substance | |
Biological Process | response to water deprivation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADPH-dependent aldo-keto reductase, chloroplastic
- EC number
- Short namesAtChlAKR
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ0PGJ6
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000400313 | 2-315 | NADPH-dependent aldo-keto reductase, chloroplastic | |||
Sequence: ANAITFFKLNTGAKFPSVGLGTWQASPGLVGDAVAAAVKIGYRHIDCAQIYGNEKEIGAVLKKLFEDRVVKREDLFITSKLWCTDHDPQDVPEALNRTLKDLQLEYVDLYLIHWPARIKKGSVGIKPENLLPVDIPSTWKAMEALYDSGKARAIGVSNFSTKKLADLLELARVPPAVNQVECHPSWRQTKLQEFCKSKGVHLSAYSPLGSPGTTWLKSDVLKNPILNMVAEKLGKSPAQVALRWGLQMGHSVLPKSTNEGRIKENFNVFDWSIPDYMFAKFAEIEQARLVTGSFLVHETLSPYKSIEELWDGEI |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Protein-protein interaction databases
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q0PGJ6-1
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
- Length315
- Mass (Da)35,137
- Last updated2006-09-05 v1
- Checksum8C0C6801749261DE
Q0PGJ6-2
- Name2
Sequence caution
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_040016 | 205-283 | in isoform 2 | |||
Sequence: AYSPLGSPGTTWLKSDVLKNPILNMVAEKLGKSPAQVALRWGLQMGHSVLPKSTNEGRIKENFNVFDWSIPDYMFAKFA → VSITRLTNPFTFYFIHSLNDFFFPGILAIRFSRDNMAEERCFEEPDTEYGCGKTRKESCASRPSLGTPNGSQCASQEYK | ||||||
Alternative sequence | VSP_040017 | 284-315 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ837654 EMBL· GenBank· DDBJ | ABH07515.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004684 EMBL· GenBank· DDBJ | AAC23647.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002685 EMBL· GenBank· DDBJ | AEC09448.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC09449.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX820913 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BT004098 EMBL· GenBank· DDBJ | AAO42123.1 EMBL· GenBank· DDBJ | mRNA |