AKRC9_ARATH
ID AKRC9_ARATH Reviewed; 315 AA.
AC Q0PGJ6; O80945; Q2V420; Q84W94;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=NADPH-dependent aldo-keto reductase, chloroplastic {ECO:0000303|PubMed:21169366};
DE Short=AtChlAKR {ECO:0000303|PubMed:21169366};
DE EC=1.1.1.- {ECO:0000269|PubMed:19616008, ECO:0000269|PubMed:21169366};
DE AltName: Full=Aldo-keto reductase family 4 member C9;
GN Name=AKR4C9; OrderedLocusNames=At2g37770; ORFNames=F13M22, T8P21.32;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (1.25
RP ANGSTROMS) IN COMPLEX WITH NADP, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND INDUCTION.
RC STRAIN=cv. Columbia; TISSUE=Flower bud;
RX PubMed=19616008; DOI=10.1016/j.jmb.2009.07.023;
RA Simpson P.J., Tantitadapitak C., Reed A.M., Mather O.C., Bunce C.M.,
RA White S.A., Ride J.P.;
RT "Characterization of two novel aldo-keto reductases from Arabidopsis:
RT expression patterns, broad substrate specificity, and an open active-site
RT structure suggest a role in toxicant metabolism following stress.";
RL J. Mol. Biol. 392:465-480(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-315 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21169366; DOI=10.1074/jbc.m110.202226;
RA Yamauchi Y., Hasegawa A., Taninaka A., Mizutani M., Sugimoto Y.;
RT "NADPH-dependent reductases involved in the detoxification of reactive
RT carbonyls in plants.";
RL J. Biol. Chem. 286:6999-7009(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Oxidoreductase acting on a broad range of substrates: reduces
CC ketosteroids, aromatic aldehydes, ketones, sugars and other aliphatic
CC aldehydes, and oxidizes hydroxysteroids (PubMed:19616008). Aldehyde
CC reductase that catalyzes the reduction of the aldehyde carbonyl groups
CC on saturated and alpha,beta-unsaturated aldehydes (PubMed:21169366). No
CC activity on alpha,beta-unsaturated ketones (PubMed:21169366). Can use
CC propionaldehyde, butyraldehyde, methylglyoxal, (E)-2-pentenal, (E)-2-
CC hexenal, (Z)-3-hexenal and (E)-2-nonenal as substrates, propenal
CC (acrolein), crotonaldehyde, but not 2-butanone, 3-buten-2-one or 1-
CC penten-3-one (PubMed:21169366). May function as detoxifiying enzyme by
CC reducing a range of toxic aldehydes and ketones produced during stress
CC (PubMed:19616008). {ECO:0000269|PubMed:19616008,
CC ECO:0000269|PubMed:21169366}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1445 uM for benzaldehyde {ECO:0000269|PubMed:19616008};
CC KM=102 uM for 3-fluorobenzaldehyde {ECO:0000269|PubMed:19616008};
CC KM=270 uM for cinnamylaldehyde {ECO:0000269|PubMed:19616008};
CC KM=261 uM for 3-hydroxybenzaldehyde {ECO:0000269|PubMed:19616008};
CC KM=82 uM for isopropylbenzaldehyde {ECO:0000269|PubMed:19616008};
CC KM=4.4 uM for 9,10-phenanthrenequinone {ECO:0000269|PubMed:19616008};
CC KM=5.49 mM for 2-E-hexenal {ECO:0000269|PubMed:19616008};
CC KM=4 mM for 4-hydroxy-2-nonenal {ECO:0000269|PubMed:19616008};
CC KM=51 mM for malondialdehyde {ECO:0000269|PubMed:19616008};
CC KM=0.46 mM for methylglyoxal {ECO:0000269|PubMed:19616008};
CC KM=2.2 mM for glyceraldehyde {ECO:0000269|PubMed:19616008};
CC KM=10.2 mM for glyoxal {ECO:0000269|PubMed:19616008};
CC KM=2.8 mM for erythrose {ECO:0000269|PubMed:19616008};
CC KM=238 mM for xylose {ECO:0000269|PubMed:19616008};
CC KM=240 mM for arabinose {ECO:0000269|PubMed:19616008};
CC KM=760 mM for glucose {ECO:0000269|PubMed:19616008};
CC KM=121 mM for galactose {ECO:0000269|PubMed:19616008};
CC KM=70 mM for propionaldehyde {ECO:0000269|PubMed:21169366};
CC KM=6.9 mM for butyraldehyde {ECO:0000269|PubMed:21169366};
CC KM=2.6 mM for acrolein {ECO:0000269|PubMed:21169366};
CC KM=1.63 mM for crotonaldehyde {ECO:0000269|PubMed:21169366};
CC KM=0.63 mM for (E)-2-pentenal {ECO:0000269|PubMed:21169366};
CC KM=0.72 mM for (E)-2-hexenal {ECO:0000269|PubMed:21169366};
CC KM=1.67 mM for (E)-2-nonenal {ECO:0000269|PubMed:21169366};
CC KM=0.24 mM for methylglyoxal {ECO:0000269|PubMed:21169366};
CC Note=kcat is 44 sec(-1) for propionaldehyde. kcat is 21 sec(-1) for
CC butyraldehyde. kcat is 6.6 sec(-1) for acrolein. kcat is 18 sec(-1)
CC for crotonaldehyde. kcat is 9.5 sec(-1) for (E)-2-pentenal. kcat is
CC 7.3 sec(-1) for (E)-2-hexenal. kcat is 7.9 sec(-1) for (E)-2-nonenal.
CC kcat is 11.5 sec(-1) for methylglyoxal.
CC {ECO:0000269|PubMed:21169366};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21169366}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0PGJ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0PGJ6-2; Sequence=VSP_040016, VSP_040017;
CC -!- INDUCTION: By drought, salt and cold stresses.
CC {ECO:0000269|PubMed:19616008}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23647.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BX820913; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; DQ837654; ABH07515.1; -; mRNA.
DR EMBL; AC004684; AAC23647.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09448.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09449.1; -; Genomic_DNA.
DR EMBL; BX820913; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT004098; AAO42123.1; -; mRNA.
DR PIR; T02543; T02543.
DR RefSeq; NP_001031505.1; NM_001036428.3. [Q0PGJ6-1]
DR RefSeq; NP_181313.3; NM_129333.3. [Q0PGJ6-2]
DR PDB; 3H7U; X-ray; 1.25 A; A=1-315.
DR PDBsum; 3H7U; -.
DR AlphaFoldDB; Q0PGJ6; -.
DR SMR; Q0PGJ6; -.
DR STRING; 3702.AT2G37770.2; -.
DR iPTMnet; Q0PGJ6; -.
DR PaxDb; Q0PGJ6; -.
DR PRIDE; Q0PGJ6; -.
DR ProteomicsDB; 244822; -. [Q0PGJ6-1]
DR EnsemblPlants; AT2G37770.1; AT2G37770.1; AT2G37770. [Q0PGJ6-2]
DR EnsemblPlants; AT2G37770.2; AT2G37770.2; AT2G37770. [Q0PGJ6-1]
DR GeneID; 818354; -.
DR Gramene; AT2G37770.1; AT2G37770.1; AT2G37770. [Q0PGJ6-2]
DR Gramene; AT2G37770.2; AT2G37770.2; AT2G37770. [Q0PGJ6-1]
DR KEGG; ath:AT2G37770; -.
DR Araport; AT2G37770; -.
DR TAIR; locus:2040646; AT2G37770.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; Q0PGJ6; -.
DR OMA; AFKPGNE; -.
DR PhylomeDB; Q0PGJ6; -.
DR BioCyc; ARA:AT2G37770-MON; -.
DR BioCyc; MetaCyc:AT2G37770-MON; -.
DR SABIO-RK; Q0PGJ6; -.
DR EvolutionaryTrace; Q0PGJ6; -.
DR PRO; PR:Q0PGJ6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q0PGJ6; baseline and differential.
DR Genevisible; Q0PGJ6; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:TAIR.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IDA:UniProtKB.
DR GO; GO:0070401; F:NADP+ binding; IDA:UniProtKB.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR CDD; cd19125; AKR_AKR4C1-15; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044498; AKR4C.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chloroplast;
KW Detoxification; NADP; Oxidoreductase; Plastid; Reference proteome;
KW Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..315
FT /note="NADPH-dependent aldo-keto reductase, chloroplastic"
FT /id="PRO_0000400313"
FT ACT_SITE 52
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 23..24
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19616008"
FT BINDING 47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19616008"
FT BINDING 114
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 158..159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19616008"
FT BINDING 180
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19616008"
FT BINDING 207..213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19616008"
FT BINDING 256..258
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19616008"
FT BINDING 262..266
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19616008"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 205..283
FT /note="AYSPLGSPGTTWLKSDVLKNPILNMVAEKLGKSPAQVALRWGLQMGHSVLPK
FT STNEGRIKENFNVFDWSIPDYMFAKFA -> VSITRLTNPFTFYFIHSLNDFFFPGILA
FT IRFSRDNMAEERCFEEPDTEYGCGKTRKESCASRPSLGTPNGSQCASQEYK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_040016"
FT VAR_SEQ 284..315
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_040017"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:3H7U"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 28..41
FT /evidence="ECO:0007829|PDB:3H7U"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:3H7U"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:3H7U"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:3H7U"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:3H7U"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:3H7U"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 238..248
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 276..281
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:3H7U"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:3H7U"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:3H7U"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:3H7U"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:3H7U"
SQ SEQUENCE 315 AA; 35137 MW; 8C0C6801749261DE CRC64;
MANAITFFKL NTGAKFPSVG LGTWQASPGL VGDAVAAAVK IGYRHIDCAQ IYGNEKEIGA
VLKKLFEDRV VKREDLFITS KLWCTDHDPQ DVPEALNRTL KDLQLEYVDL YLIHWPARIK
KGSVGIKPEN LLPVDIPSTW KAMEALYDSG KARAIGVSNF STKKLADLLE LARVPPAVNQ
VECHPSWRQT KLQEFCKSKG VHLSAYSPLG SPGTTWLKSD VLKNPILNMV AEKLGKSPAQ
VALRWGLQMG HSVLPKSTNE GRIKENFNVF DWSIPDYMFA KFAEIEQARL VTGSFLVHET
LSPYKSIEEL WDGEI
