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Protein

NADPH-dependent aldo-keto reductase, chloroplastic

Gene

AKR4C9

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).2 Publications

Kineticsi

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.1 Publication
  1. KM=1445 µM for benzaldehyde1 Publication
  2. KM=102 µM for 3-fluorobenzaldehyde1 Publication
  3. KM=270 µM for cinnamylaldehyde1 Publication
  4. KM=261 µM for 3-hydroxybenzaldehyde1 Publication
  5. KM=82 µM for isopropylbenzaldehyde1 Publication
  6. KM=4.4 µM for 9,10-phenanthrenequinone1 Publication
  7. KM=5.49 mM for 2-E-hexenal1 Publication
  8. KM=4 mM for 4-hydroxy-2-nonenal1 Publication
  9. KM=51 mM for malondialdehyde1 Publication
  10. KM=0.46 mM for methylglyoxal1 Publication
  11. KM=2.2 mM for glyceraldehyde1 Publication
  12. KM=10.2 mM for glyoxal1 Publication
  13. KM=2.8 mM for erythrose1 Publication
  14. KM=238 mM for xylose1 Publication
  15. KM=240 mM for arabinose1 Publication
  16. KM=760 mM for glucose1 Publication
  17. KM=121 mM for galactose1 Publication
  18. KM=70 mM for propionaldehyde1 Publication
  19. KM=6.9 mM for butyraldehyde1 Publication
  20. KM=2.6 mM for acrolein1 Publication
  21. KM=1.63 mM for crotonaldehyde1 Publication
  22. KM=0.63 mM for (E)-2-pentenal1 Publication
  23. KM=0.72 mM for (E)-2-hexenal1 Publication
  24. KM=1.67 mM for (E)-2-nonenal1 Publication
  25. KM=0.24 mM for methylglyoxal1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei47NADP1 Publication1
    Active sitei52Proton donorBy similarity1
    Binding sitei114NADPBy similarity1
    Binding sitei180NADP1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi23 – 24NADP1 Publication2
    Nucleotide bindingi158 – 159NADP1 Publication2
    Nucleotide bindingi207 – 213NADP1 Publication7
    Nucleotide bindingi256 – 258NADP1 Publication3
    Nucleotide bindingi262 – 266NADP1 Publication5

    GO - Molecular functioni

    • alcohol dehydrogenase (NADP+) activity Source: TAIR
    • aldo-keto reductase (NADP) activity Source: UniProtKB
    • NADP+ binding Source: UniProtKB
    • steroid dehydrogenase activity Source: UniProtKB

    GO - Biological processi

    • oxidation-reduction process Source: TAIR
    • response to cold Source: UniProtKB
    • response to salt stress Source: UniProtKB
    • response to toxic substance Source: UniProtKB-KW
    • response to water deprivation Source: UniProtKB

    Keywordsi

    Molecular functionOxidoreductase
    Biological processDetoxification, Stress response
    LigandNADP

    Enzyme and pathway databases

    BioCyciARA:AT2G37770-MONOMER.
    MetaCyc:AT2G37770-MONOMER.
    ReactomeiR-ATH-156590. Glutathione conjugation.
    R-ATH-193144. Estrogen biosynthesis.
    R-ATH-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    R-ATH-193775. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    R-ATH-193807. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
    R-ATH-196108. Pregnenolone biosynthesis.
    R-ATH-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    R-ATH-5365859. RA biosynthesis pathway.
    R-ATH-5652227. Fructose biosynthesis.
    R-ATH-5661270. Catabolism of glucuronate to xylulose-5-phosphate.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH-dependent aldo-keto reductase, chloroplastic1 Publication (EC:1.1.1.-2 Publications)
    Short name:
    AtChlAKR1 Publication
    Alternative name(s):
    Aldo-keto reductase family 4 member C9
    Gene namesi
    Name:AKR4C9
    Ordered Locus Names:At2g37770
    ORF Names:F13M22, T8P21.32
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 2

    Organism-specific databases

    AraportiAT2G37770.
    TAIRilocus:2040646. AT2G37770.

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00004003132 – 315NADPH-dependent aldo-keto reductase, chloroplasticAdd BLAST314

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineCombined sources1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ0PGJ6.

    Expressioni

    Inductioni

    By drought, salt and cold stresses.1 Publication

    Gene expression databases

    ExpressionAtlasiQ0PGJ6. baseline and differential.
    GenevisibleiQ0PGJ6. AT.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT2G37770.2.

    Structurei

    Secondary structure

    1315
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi7 – 9Combined sources3
    Beta strandi15 – 19Combined sources5
    Helixi28 – 41Combined sources14
    Beta strandi45 – 47Combined sources3
    Helixi50 – 52Combined sources3
    Helixi55 – 67Combined sources13
    Helixi73 – 75Combined sources3
    Beta strandi77 – 82Combined sources6
    Helixi84 – 86Combined sources3
    Helixi91 – 103Combined sources13
    Beta strandi108 – 113Combined sources6
    Helixi128 – 130Combined sources3
    Helixi136 – 148Combined sources13
    Beta strandi151 – 159Combined sources9
    Helixi162 – 171Combined sources10
    Beta strandi177 – 182Combined sources6
    Helixi190 – 199Combined sources10
    Beta strandi202 – 207Combined sources6
    Helixi221 – 223Combined sources3
    Helixi225 – 234Combined sources10
    Helixi238 – 248Combined sources11
    Helixi260 – 267Combined sources8
    Helixi276 – 281Combined sources6
    Helixi282 – 284Combined sources3
    Helixi294 – 296Combined sources3
    Turni299 – 301Combined sources3
    Beta strandi302 – 306Combined sources5
    Helixi307 – 310Combined sources4
    Turni311 – 313Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3H7UX-ray1.25A1-315[»]
    ProteinModelPortaliQ0PGJ6.
    SMRiQ0PGJ6.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ0PGJ6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiKOG1577. Eukaryota.
    COG0656. LUCA.
    HOGENOMiHOG000250272.
    InParanoidiQ0PGJ6.
    OMAiKDTWAAM.
    OrthoDBiEOG09360F0E.
    PhylomeDBiQ0PGJ6.

    Family and domain databases

    CDDicd06660. Aldo_ket_red. 1 hit.
    Gene3Di3.20.20.100. 1 hit.
    InterProiView protein in InterPro
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    PfamiView protein in Pfam
    PF00248. Aldo_ket_red. 1 hit.
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiView protein in PROSITE
    PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q0PGJ6-1) [UniParc]FASTAAdd to basket

    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.

    « Hide

            10         20         30         40         50
    MANAITFFKL NTGAKFPSVG LGTWQASPGL VGDAVAAAVK IGYRHIDCAQ
    60 70 80 90 100
    IYGNEKEIGA VLKKLFEDRV VKREDLFITS KLWCTDHDPQ DVPEALNRTL
    110 120 130 140 150
    KDLQLEYVDL YLIHWPARIK KGSVGIKPEN LLPVDIPSTW KAMEALYDSG
    160 170 180 190 200
    KARAIGVSNF STKKLADLLE LARVPPAVNQ VECHPSWRQT KLQEFCKSKG
    210 220 230 240 250
    VHLSAYSPLG SPGTTWLKSD VLKNPILNMV AEKLGKSPAQ VALRWGLQMG
    260 270 280 290 300
    HSVLPKSTNE GRIKENFNVF DWSIPDYMFA KFAEIEQARL VTGSFLVHET
    310
    LSPYKSIEEL WDGEI
    Length:315
    Mass (Da):35,137
    Last modified:September 5, 2006 - v1
    Checksum:i8C0C6801749261DE
    GO
    Isoform 2 (identifier: Q0PGJ6-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         205-283: AYSPLGSPGT...IPDYMFAKFA → VSITRLTNPF...GSQCASQEYK
         284-315: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:283
    Mass (Da):31,680
    Checksum:i30F92CE11A5D95F0
    GO

    Sequence cautioni

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

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_040016205 – 283AYSPL…FAKFA → VSITRLTNPFTFYFIHSLND FFFPGILAIRFSRDNMAEER CFEEPDTEYGCGKTRKESCA SRPSLGTPNGSQCASQEYK in isoform 2. 1 PublicationAdd BLAST79
    Alternative sequenceiVSP_040017284 – 315Missing in isoform 2. 1 PublicationAdd BLAST32

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    DQ837654 mRNA. Translation: ABH07515.1.
    AC004684 Genomic DNA. Translation: AAC23647.1. Sequence problems.
    CP002685 Genomic DNA. Translation: AEC09448.1.
    CP002685 Genomic DNA. Translation: AEC09449.1.
    BX820913 mRNA. No translation available.
    BT004098 mRNA. Translation: AAO42123.1.
    PIRiT02543.
    RefSeqiNP_001031505.1. NM_001036428.3. [Q0PGJ6-1]
    NP_181313.3. NM_129333.3. [Q0PGJ6-2]
    UniGeneiAt.12803.

    Genome annotation databases

    EnsemblPlantsiAT2G37770.1; AT2G37770.1; AT2G37770. [Q0PGJ6-2]
    AT2G37770.2; AT2G37770.2; AT2G37770. [Q0PGJ6-1]
    GeneIDi818354.
    GrameneiAT2G37770.1; AT2G37770.1; AT2G37770.
    AT2G37770.2; AT2G37770.2; AT2G37770.
    KEGGiath:AT2G37770.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Similar proteinsi

    Entry informationi

    Entry nameiAKRC9_ARATH
    AccessioniPrimary (citable) accession number: Q0PGJ6
    Secondary accession number(s): O80945, Q2V420, Q84W94
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 2, 2010
    Last sequence update: September 5, 2006
    Last modified: September 27, 2017
    This is version 83 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families