Q0PGJ6 · AKRC9_ARATH

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).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
1445 μMbenzaldehyde
102 μM3-fluorobenzaldehyde
270 μMcinnamylaldehyde
261 μM3-hydroxybenzaldehyde
82 μMisopropylbenzaldehyde
4.4 μM9,10-phenanthrenequinone
5.49 mM2-E-hexenal
4 mM4-hydroxy-2-nonenal
51 mMmalondialdehyde
0.46 mMmethylglyoxal
2.2 mMglyceraldehyde
10.2 mMglyoxal
2.8 mMerythrose
238 mMxylose
240 mMarabinose
760 mMglucose
121 mMgalactose
70 mMpropionaldehyde
6.9 mMbutyraldehyde
2.6 mMacrolein
1.63 mMcrotonaldehyde
0.63 mM(E)-2-pentenal
0.72 mM(E)-2-hexenal
1.67 mM(E)-2-nonenal
0.24 mMmethylglyoxal
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.

TypeIDPosition(s)Description
Binding site23-24NADP+ (UniProtKB | ChEBI)
Binding site47NADP+ (UniProtKB | ChEBI)
Active site52Proton donor
Binding site114NADP+ (UniProtKB | ChEBI)
Binding site158-159NADP+ (UniProtKB | ChEBI)
Binding site180NADP+ (UniProtKB | ChEBI)
Binding site207-213NADP+ (UniProtKB | ChEBI)
Binding site256-258NADP+ (UniProtKB | ChEBI)
Binding site262-266NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchloroplast
Cellular Componentendoplasmic reticulum
Molecular Functionalcohol dehydrogenase (NADP+) activity
Molecular Functionaldo-keto reductase (NADPH) activity
Molecular FunctionNADP+ binding
Molecular Functionsteroid dehydrogenase activity
Biological Processresponse to cold
Biological Processresponse to salt stress
Biological Processresponse to toxic substance
Biological Processresponse to water deprivation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    NADPH-dependent aldo-keto reductase, chloroplastic
  • EC number
  • Short names
    AtChlAKR
  • Alternative names
    • Aldo-keto reductase family 4 member C9

Gene names

    • Name
      AKR4C9
    • ORF names
      F13M22, T8P21.32
    • Ordered locus names
      At2g37770

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q0PGJ6
  • Secondary accessions
    • O80945
    • Q2V420
    • Q84W94

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00004003132-315NADPH-dependent aldo-keto reductase, chloroplastic

Keywords

Proteomic databases

PTM databases

Expression

Induction

By drought, salt and cold stresses.

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the aldo/keto reductase family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

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.

  • Length
    315
  • Mass (Da)
    35,137
  • Last updated
    2006-09-05 v1
  • Checksum
    8C0C6801749261DE
MANAITFFKLNTGAKFPSVGLGTWQASPGLVGDAVAAAVKIGYRHIDCAQIYGNEKEIGAVLKKLFEDRVVKREDLFITSKLWCTDHDPQDVPEALNRTLKDLQLEYVDLYLIHWPARIKKGSVGIKPENLLPVDIPSTWKAMEALYDSGKARAIGVSNFSTKKLADLLELARVPPAVNQVECHPSWRQTKLQEFCKSKGVHLSAYSPLGSPGTTWLKSDVLKNPILNMVAEKLGKSPAQVALRWGLQMGHSVLPKSTNEGRIKENFNVFDWSIPDYMFAKFAEIEQARLVTGSFLVHETLSPYKSIEELWDGEI

Q0PGJ6-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 205-283: AYSPLGSPGTTWLKSDVLKNPILNMVAEKLGKSPAQVALRWGLQMGHSVLPKSTNEGRIKENFNVFDWSIPDYMFAKFA → VSITRLTNPFTFYFIHSLNDFFFPGILAIRFSRDNMAEERCFEEPDTEYGCGKTRKESCASRPSLGTPNGSQCASQEYK
    • 284-315: Missing

Sequence caution

The sequence AAC23647.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence BX820913 differs from that shown. Reason: Miscellaneous discrepancy Sequencing errors.

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_040016205-283in isoform 2
Alternative sequenceVSP_040017284-315in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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