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Protein

Aldo-keto reductase family 4 member C9

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. May function as detoxifiying enzyme by reducing a range of toxic aldehydes and ketones produced during stress.1 Publication

Kineticsi

  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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei47 – 471NADP1 Publication
    Active sitei52 – 521Proton donorBy similarity
    Binding sitei114 – 1141NADPBy similarity
    Binding sitei180 – 1801NADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi23 – 242NADP1 Publication
    Nucleotide bindingi158 – 1592NADP1 Publication
    Nucleotide bindingi207 – 2137NADP1 Publication
    Nucleotide bindingi256 – 2583NADP1 Publication
    Nucleotide bindingi262 – 2665NADP1 Publication

    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
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Detoxification, Stress response

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciARA:AT2G37770-MONOMER.
    ARA:GQT-1604-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:
    Aldo-keto reductase family 4 member C9 (EC:1.1.1.-)
    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

    TAIRiAT2G37770.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: TAIR
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemovedCombined sources
    Chaini2 – 315314Aldo-keto reductase family 4 member C9PRO_0000400313Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineCombined sources

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ0PGJ6.
    PRIDEiQ0PGJ6.

    Expressioni

    Inductioni

    By drought, salt and cold stresses.1 Publication

    Gene expression databases

    GenevisibleiQ0PGJ6. AT.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT2G37770.2.

    Structurei

    Secondary structure

    1
    315
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 93Combined sources
    Beta strandi15 – 195Combined sources
    Helixi28 – 4114Combined sources
    Beta strandi45 – 473Combined sources
    Helixi50 – 523Combined sources
    Helixi55 – 6713Combined sources
    Helixi73 – 753Combined sources
    Beta strandi77 – 826Combined sources
    Helixi84 – 863Combined sources
    Helixi91 – 10313Combined sources
    Beta strandi108 – 1136Combined sources
    Helixi128 – 1303Combined sources
    Helixi136 – 14813Combined sources
    Beta strandi151 – 1599Combined sources
    Helixi162 – 17110Combined sources
    Beta strandi177 – 1826Combined sources
    Helixi190 – 19910Combined sources
    Beta strandi202 – 2076Combined sources
    Helixi221 – 2233Combined sources
    Helixi225 – 23410Combined sources
    Helixi238 – 24811Combined sources
    Helixi260 – 2678Combined sources
    Helixi276 – 2816Combined sources
    Helixi282 – 2843Combined sources
    Helixi294 – 2963Combined sources
    Turni299 – 3013Combined sources
    Beta strandi302 – 3065Combined sources
    Helixi307 – 3104Combined sources
    Turni311 – 3133Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3H7UX-ray1.25A1-315[»]
    ProteinModelPortaliQ0PGJ6.
    SMRiQ0PGJ6. Positions 4-315.
    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.
    OMAiFEDRVVK.
    PhylomeDBiQ0PGJ6.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]

    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 AAC23647.1 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)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei205 – 28379AYSPL…FAKFA → VSITRLTNPFTFYFIHSLND FFFPGILAIRFSRDNMAEER CFEEPDTEYGCGKTRKESCA SRPSLGTPNGSQCASQEYK in isoform 2. 1 PublicationVSP_040016Add
    BLAST
    Alternative sequencei284 – 31532Missing in isoform 2. 1 PublicationVSP_040017Add
    BLAST

    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_001036428.2. [Q0PGJ6-1]
    NP_181313.3. NM_129333.3. [Q0PGJ6-2]
    UniGeneiAt.12803.

    Genome annotation databases

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

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    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_001036428.2. [Q0PGJ6-1]
    NP_181313.3. NM_129333.3. [Q0PGJ6-2]
    UniGeneiAt.12803.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3H7UX-ray1.25A1-315[»]
    ProteinModelPortaliQ0PGJ6.
    SMRiQ0PGJ6. Positions 4-315.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi3702.AT2G37770.2.

    Proteomic databases

    PaxDbiQ0PGJ6.
    PRIDEiQ0PGJ6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    TAIRiAT2G37770.

    Phylogenomic databases

    eggNOGiKOG1577. Eukaryota.
    COG0656. LUCA.
    HOGENOMiHOG000250272.
    InParanoidiQ0PGJ6.
    OMAiFEDRVVK.
    PhylomeDBiQ0PGJ6.

    Enzyme and pathway databases

    BioCyciARA:AT2G37770-MONOMER.
    ARA:GQT-1604-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.

    Miscellaneous databases

    EvolutionaryTraceiQ0PGJ6.
    PROiQ0PGJ6.

    Gene expression databases

    GenevisibleiQ0PGJ6. AT.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Characterization of two novel aldo-keto reductases from Arabidopsis: expression patterns, broad substrate specificity, and an open active-site structure suggest a role in toxicant metabolism following stress."
      Simpson P.J., Tantitadapitak C., Reed A.M., Mather O.C., Bunce C.M., White S.A., Ride J.P.
      J. Mol. Biol. 392:465-480(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH NADP, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
      Strain: cv. Columbia.
      Tissue: Flower bud.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation."
      Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M.
      Genome Res. 14:406-413(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: cv. Columbia.
    5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-315 (ISOFORM 1).
      Strain: cv. Columbia.
    6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAKRC9_ARATH
    AccessioniPrimary (citable) accession number: Q0PGJ6
    Secondary accession number(s): O80945, Q2V420, Q84W94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 2, 2010
    Last sequence update: September 5, 2006
    Last modified: December 9, 2015
    This is version 72 of the entry and version 1 of the sequence. [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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.