ID AER_ARATH Reviewed; 345 AA.
AC Q39172; Q501A9; Q8L865;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 156.
DE RecName: Full=NADPH-dependent oxidoreductase 2-alkenal reductase {ECO:0000303|PubMed:16299173};
DE Short=AtAER {ECO:0000303|PubMed:16299173};
DE EC=1.3.1.- {ECO:0000269|PubMed:10848984};
DE EC=1.3.1.74 {ECO:0000269|PubMed:12514241, ECO:0000269|PubMed:16299173, ECO:0000269|PubMed:17028190, ECO:0000269|PubMed:26678323};
DE AltName: Full=NADP-dependent alkenal double bond reductase P1 {ECO:0000303|PubMed:17028190};
DE Short=DBR1 {ECO:0000303|PubMed:17028190};
DE AltName: Full=NADPH-azodicarbonyl/quinone reductase {ECO:0000303|PubMed:10848984};
DE AltName: Full=NADPH:2-alkenal/one alpha,beta-hydrogenase {ECO:0000303|PubMed:12514241};
DE Short=ALH {ECO:0000303|PubMed:12514241};
DE AltName: Full=P1-zeta-crystallin protein {ECO:0000303|PubMed:7592828};
DE Short=P1-ZCr {ECO:0000303|PubMed:7592828};
GN Name=AER {ECO:0000303|PubMed:16299173};
GN Synonyms=P1 {ECO:0000303|PubMed:7592828};
GN OrderedLocusNames=At5g16970 {ECO:0000312|Araport:AT5G16970};
GN ORFNames=F2K13_120 {ECO:0000312|EMBL:CAC01710.1};
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], AND INDUCTION BY OXIDATIVE STRESS.
RC STRAIN=cv. Columbia;
RX PubMed=7592828; DOI=10.1074/jbc.270.44.26224;
RA Babiychuk E., Kushnir S., Belles-Boix E., van Montagu M., Inze D.;
RT "Arabidopsis thaliana NADPH oxidoreductase homologs confer tolerance of
RT yeasts toward the thiol-oxidizing drug diamide.";
RL J. Biol. Chem. 270:26224-26231(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP ACTIVITY REGULATION.
RX PubMed=10848984; DOI=10.1046/j.1432-1327.2000.01398.x;
RA Mano J., Babiychuk E., Belles-Boix E., Hiratake J., Kimura A., Inze D.,
RA Kushnir S., Asada K.;
RT "A novel NADPH:diamide oxidoreductase activity in arabidopsis thaliana P1
RT zeta-crystallin.";
RL Eur. J. Biochem. 267:3661-3671(2000).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=12514241; DOI=10.1093/pcp/pcf187;
RA Mano J., Torii Y., Hayashi S., Takimoto K., Matsui K., Nakamura K.,
RA Inze D., Babiychuk E., Kushnir S., Asada K.;
RT "The NADPH:quinone oxidoreductase P1-zeta-crystallin in Arabidopsis
RT catalyzes the alpha,beta-hydrogenation of 2-alkenals: detoxication of the
RT lipid peroxide-derived reactive aldehydes.";
RL Plant Cell Physiol. 43:1445-1455(2002).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=16299173; DOI=10.1104/pp.105.070391;
RA Mano J., Belles-Boix E., Babiychuk E., Inze D., Torii Y., Hiraoka E.,
RA Takimoto K., Slooten L., Asada K., Kushnir S.;
RT "Protection against photooxidative injury of tobacco leaves by 2-alkenal
RT reductase. Detoxication of lipid peroxide-derived reactive carbonyls.";
RL Plant Physiol. 139:1773-1783(2005).
RN [9]
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=26678323; DOI=10.1016/j.phytochem.2015.11.015;
RA Curien G., Giustini C., Montillet J.L., Mas-Y-Mas S., Cobessi D.,
RA Ferrer J.L., Matringe M., Grechkin A., Rolland N.;
RT "The chloroplast membrane associated ceQORH putative quinone oxidoreductase
RT reduces long-chain, stress-related oxidized lipids.";
RL Phytochemistry 122:45-55(2016).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES AND
RP NADP, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=17028190; DOI=10.1074/jbc.m605900200;
RA Youn B., Kim S.J., Moinuddin S.G., Lee C., Bedgar D.L., Harper A.R.,
RA Davin L.B., Lewis N.G., Kang C.;
RT "Mechanistic and structural studies of apoform, binary, and ternary
RT complexes of the Arabidopsis alkenal double bond reductase At5g16970.";
RL J. Biol. Chem. 281:40076-40088(2006).
CC -!- FUNCTION: Involved in the detoxification of reactive carbonyls
CC (PubMed:10848984, PubMed:12514241, PubMed:16299173). Acts on lipid
CC peroxide-derived reactive aldehydes (PubMed:12514241). Specific to a
CC double bond activated by an adjacent carbonyl group (PubMed:12514241).
CC Can use both quinones and diamide as substrates, but not menadione,
CC ferricyanide or phylloquinone (PubMed:10848984). Can use 4-hydroxy-
CC (2E)-nonenal (HNE), 4-hydroxy-(2E)-hexenal (HHE), (2E)-nonenal, (2E)-
CC hexenal, (2E)-pentenal, propenal (acrolein), 3-buten-2-one and 3-
CC penten-2-one, but not (R)-(-)-carvone, n-nonanal, n-hexanal, (3Z)-
CC hexanal, cyclohex-2-en-1-one or 12-oxo phytodienoic acid (OPDA) as
CC electron acceptors (PubMed:12514241). Catalyzes the reduction of the
CC alpha,beta-unsaturated bond of 2-alkenals, of lipid peroxide-derived
CC oxenes 9-oxo-10(E),12(Z)-octadecadienoic acid (9-KODE) and 13-oxo-
CC 9(Z),11(E)-octadecadienoic acid (13-KODE), as well as 4-oxo-(2E)-
CC nonenal and 4-hydroxynonenal (PubMed:16299173). Can use 12-oxo-10(E)
CC dodecanoate (traumatin), trans-1,3 diphenyl-2-propenone, trans-1,4-
CC diphenyl-2-butene-1,4-dione, 9-oxo-12,13-epoxy-(10E)-octadecenoic acid
CC (trans-EKODE-1b) and 9,13-dihydroxy-10-oxo-11-octadecenoic acid as
CC substrates (PubMed:26678323). Catalyzes the reduction of the 7-8 double
CC bond of phenylpropanal substrates, such as p-coumaryl aldehyde and
CC coniferyl aldehyde (in vitro) (PubMed:17028190). Has activity towards
CC toxic substrates, such as 4-hydroxy-(2E)-nonenal (in vitro)
CC (PubMed:17028190). May play a distinct role in plant antioxidant
CC defense and is possibly involved in NAD(P)/NAD(P)H homeostasis
CC (PubMed:17028190). {ECO:0000269|PubMed:10848984,
CC ECO:0000269|PubMed:12514241, ECO:0000269|PubMed:16299173,
CC ECO:0000269|PubMed:17028190, ECO:0000269|PubMed:26678323}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an n-alkanal + NAD(+) = an alk-2-enal + H(+) + NADH;
CC Xref=Rhea:RHEA:13733, ChEBI:CHEBI:12834, ChEBI:CHEBI:13757,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.74;
CC Evidence={ECO:0000269|PubMed:12514241, ECO:0000269|PubMed:16299173,
CC ECO:0000269|PubMed:17028190, ECO:0000269|PubMed:26678323};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an n-alkanal + NADP(+) = an alk-2-enal + H(+) + NADPH;
CC Xref=Rhea:RHEA:13737, ChEBI:CHEBI:12834, ChEBI:CHEBI:13757,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.74;
CC Evidence={ECO:0000269|PubMed:12514241, ECO:0000269|PubMed:16299173,
CC ECO:0000269|PubMed:17028190, ECO:0000269|PubMed:26678323};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide and p-
CC chloromercuribenzoic acid. {ECO:0000269|PubMed:10848984}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.53 mM for p-coumaryl aldehyde {ECO:0000269|PubMed:17028190};
CC KM=0.41 mM for coniferyl aldehyde {ECO:0000269|PubMed:17028190};
CC KM=0.28 mM for 4-hydroxy-(2E)-nonenal {ECO:0000269|PubMed:17028190};
CC KM=10 uM for trans-1,3 diphenyl-2-propenone
CC {ECO:0000269|PubMed:26678323};
CC KM=3.7 uM for trans-1,4-diphenyl-2-butene-1,4-dione
CC {ECO:0000269|PubMed:26678323};
CC KM=6.6 uM for traumatin {ECO:0000269|PubMed:26678323};
CC KM=0.65 uM for 9,10-phenanthrenequinone
CC {ECO:0000269|PubMed:10848984};
CC KM=11 uM for 5-Hydroxy-1,4-naphtoquinone
CC {ECO:0000269|PubMed:10848984};
CC KM=152 uM for 1,4-Benzoquinone {ECO:0000269|PubMed:10848984};
CC KM=25 uM for decyl-plastoquinone {ECO:0000269|PubMed:10848984};
CC KM=20 uM for ferricytochrome c {ECO:0000269|PubMed:10848984};
CC KM=128 uM for azodicarboxylic acid bis[dimethylamide]
CC {ECO:0000269|PubMed:10848984};
CC KM=120 uM for 1,10-(azocarbonyl)-dipeperidine
CC {ECO:0000269|PubMed:10848984};
CC KM=3.4 uM for azocarbonamide {ECO:0000269|PubMed:10848984};
CC KM=2.5 uM for NADPH for 9,10-phenanthrenequinone-reduction
CC {ECO:0000269|PubMed:10848984};
CC KM=8.2 uM for NADPH for azodicarboxylic acid bis[dimethylamide]-
CC reduction {ECO:0000269|PubMed:10848984};
CC KM=13.4 uM for 4-hydroxy-(2E)-nonenal {ECO:0000269|PubMed:12514241};
CC KM=145 uM for 4-hydroxy-(2E)-hexenal {ECO:0000269|PubMed:12514241};
CC KM=5.9 uM for (2E)-nonenal {ECO:0000269|PubMed:12514241};
CC KM=232 uM for (2E)-hexenal {ECO:0000269|PubMed:12514241};
CC KM=1420 uM for (2E)-pentenal {ECO:0000269|PubMed:12514241};
CC KM=4650 uM for propenal {ECO:0000269|PubMed:12514241};
CC KM=55 uM for 3-buten-2-one {ECO:0000269|PubMed:12514241};
CC KM=5.2 uM for 3-penten-2-one {ECO:0000269|PubMed:12514241};
CC KM=11.3 uM for (2E),(6Z)-nonadienal {ECO:0000269|PubMed:16299173};
CC KM=1.24 uM for 4-oxo-(2E)-nonenal {ECO:0000269|PubMed:16299173};
CC KM=10.0 uM for 9-oxo-10(E),12(Z)-octadecadienoic acid
CC {ECO:0000269|PubMed:16299173};
CC KM=3.92 uM for 13-oxo-9(Z),11(E)-octadecadienoic acid
CC {ECO:0000269|PubMed:16299173};
CC KM=0.673 uM for 3-nonen-2-one {ECO:0000269|PubMed:16299173};
CC Note=kcat is 3.8 sec(-1) for trans-1,3 diphenyl-2-propenone. kcat is
CC 4.9 sec(-1) for trans-1,4-diphenyl-2-butene-1,4-dione. kcat is 10
CC sec(-1) for traumatin (PubMed:26678323). kcat is 98 sec(-1) for 9,10-
CC phenanthrenequinone. kcat is 1.9 sec(-1) for 5-Hydroxy-1,4-
CC naphtoquinone. kcat is 12 sec(-1) for 1,4-Benzoquinone. kcat is 0.10
CC sec(-1) for decyl-plastoquinone. kcat is 0.03 sec(-1) for
CC ferricytochrome c. kcat is 95 sec(-1) for azodicarboxylic acid
CC bis[dimethylamide]. kcat is 42 sec(-1) for 1,10-(azocarbonyl)-
CC dipeperidine. kcat is 31 sec(-1) for azocarbonamide
CC (PubMed:10848984). kcat is 88 sec(-1) for 4-hydroxy-(2E)-nonenal.
CC kcat is 42 sec(-1) for 4-hydroxy-(2E)-hexenal. kcat is 51 sec(-1) for
CC (2E)-nonenal. kcat is 63 sec(-1) for (2E)-hexenal. kcat is 35 sec(-1)
CC for (2E)-pentenal. kcat is 40 sec(-1) for propenal. kcat is 83 sec(-
CC 1) for 3-buten-2-one. kcat is 103 sec(-1) for 3-penten-2-one
CC (PubMed:12514241). kcat is 33.9 sec(-1) for (2E),(6Z)-nonadienal.
CC kcat is 20.1 sec(-1) for 4-oxo-(2E)-nonenal. kcat is 0.94 sec(-1) for
CC 9-oxo-10(E),12(Z)-octadecadienoic acid. kcat is 1.10 sec(-1) for 13-
CC oxo-9(Z),11(E)-octadecadienoic acid. kcat is 18.9 sec(-1) for 3-
CC nonen-2-one (PubMed:16299173). {ECO:0000269|PubMed:10848984,
CC ECO:0000269|PubMed:12514241, ECO:0000269|PubMed:16299173,
CC ECO:0000269|PubMed:26678323};
CC pH dependence:
CC Optimum pH is 8.0 for 9,10-phenanthrenequinone-reduction. Optimum pH
CC is 6.5-7.0 for azodicarboxylic acid bis[dimethylamide]-reduction
CC (PubMed:10848984). Optimum pH is 6.0 with (2E)-hexenal or 4-hydroxy-
CC (2E)-nonenal as substrate (PubMed:12514241).
CC {ECO:0000269|PubMed:10848984, ECO:0000269|PubMed:12514241};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10848984,
CC ECO:0000269|PubMed:17028190}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16299173}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:16299173}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:16299173}.
CC -!- INDUCTION: Up-regulated upon treatment with paraquat, t-
CC butylhydroperoxide, diamide, and menadione.
CC {ECO:0000269|PubMed:7592828}.
CC -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC {ECO:0000305}.
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DR EMBL; Z49768; CAA89838.1; -; mRNA.
DR EMBL; AL391141; CAC01710.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92364.1; -; Genomic_DNA.
DR EMBL; AY120718; AAM53276.1; -; mRNA.
DR EMBL; BT022058; AAY25470.1; -; mRNA.
DR PIR; S57611; S57611.
DR RefSeq; NP_197199.1; NM_121703.4.
DR PDB; 2J3H; X-ray; 2.50 A; A/B=1-345.
DR PDB; 2J3I; X-ray; 2.80 A; A/B=1-345.
DR PDB; 2J3J; X-ray; 2.80 A; A/B=1-345.
DR PDB; 2J3K; X-ray; 2.80 A; A/B=1-345.
DR PDBsum; 2J3H; -.
DR PDBsum; 2J3I; -.
DR PDBsum; 2J3J; -.
DR PDBsum; 2J3K; -.
DR AlphaFoldDB; Q39172; -.
DR SMR; Q39172; -.
DR BioGRID; 16836; 2.
DR IntAct; Q39172; 1.
DR STRING; 3702.Q39172; -.
DR iPTMnet; Q39172; -.
DR PaxDb; 3702-AT5G16970-1; -.
DR ProteomicsDB; 244727; -.
DR DNASU; 831560; -.
DR EnsemblPlants; AT5G16970.1; AT5G16970.1; AT5G16970.
DR GeneID; 831560; -.
DR Gramene; AT5G16970.1; AT5G16970.1; AT5G16970.
DR KEGG; ath:AT5G16970; -.
DR Araport; AT5G16970; -.
DR TAIR; AT5G16970; AER.
DR eggNOG; KOG1196; Eukaryota.
DR HOGENOM; CLU_026673_29_1_1; -.
DR InParanoid; Q39172; -.
DR OMA; MELRIST; -.
DR OrthoDB; 640541at2759; -.
DR PhylomeDB; Q39172; -.
DR BioCyc; ARA:AT5G16970-MONOMER; -.
DR BioCyc; MetaCyc:AT5G16970-MONOMER; -.
DR SABIO-RK; Q39172; -.
DR EvolutionaryTrace; Q39172; -.
DR PRO; PR:Q39172; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39172; baseline and differential.
DR Genevisible; Q39172; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IDA:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR CDD; cd08295; double_bond_reductase_like; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR041694; ADH_N_2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR045010; MDR_fam.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43205:SF30; NADP-DEPENDENT ALKENAL DOUBLE BOND REDUCTASE P2-RELATED; 1.
DR PANTHER; PTHR43205; PROSTAGLANDIN REDUCTASE; 1.
DR Pfam; PF16884; ADH_N_2; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NADP; Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..345
FT /note="NADPH-dependent oxidoreductase 2-alkenal reductase"
FT /id="PRO_0000218073"
FT BINDING 52..53
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007744|PDB:2J3I"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:2J3K"
FT BINDING 163..169
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007744|PDB:2J3I, ECO:0007744|PDB:2J3J,
FT ECO:0007744|PDB:2J3K"
FT BINDING 188
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007744|PDB:2J3I, ECO:0007744|PDB:2J3J,
FT ECO:0007744|PDB:2J3K"
FT BINDING 192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007744|PDB:2J3I, ECO:0007744|PDB:2J3J,
FT ECO:0007744|PDB:2J3K"
FT BINDING 208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007744|PDB:2J3I, ECO:0007744|PDB:2J3J,
FT ECO:0007744|PDB:2J3K"
FT BINDING 232
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007744|PDB:2J3J"
FT BINDING 254
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007744|PDB:2J3I, ECO:0007744|PDB:2J3J,
FT ECO:0007744|PDB:2J3K"
FT BINDING 260
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007744|PDB:2J3I, ECO:0007744|PDB:2J3J,
FT ECO:0007744|PDB:2J3K"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:2J3K"
FT BINDING 284..286
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007744|PDB:2J3I, ECO:0007744|PDB:2J3J,
FT ECO:0007744|PDB:2J3K"
FT BINDING 330
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007744|PDB:2J3J, ECO:0007744|PDB:2J3K"
FT BINDING 334..336
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007744|PDB:2J3I, ECO:0007744|PDB:2J3J,
FT ECO:0007744|PDB:2J3K"
FT CONFLICT 223
FT /note="P -> T (in Ref. 4; AAM53276)"
FT /evidence="ECO:0000305"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:2J3H"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:2J3H"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2J3H"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:2J3H"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:2J3H"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:2J3H"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2J3H"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:2J3H"
FT TURN 63..68
FT /evidence="ECO:0007829|PDB:2J3H"
FT STRAND 79..89
FT /evidence="ECO:0007829|PDB:2J3H"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:2J3J"
FT STRAND 99..112
FT /evidence="ECO:0007829|PDB:2J3H"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2J3H"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:2J3H"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:2J3H"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:2J3H"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:2J3H"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:2J3I"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:2J3H"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:2J3H"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:2J3H"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:2J3H"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:2J3H"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:2J3I"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:2J3H"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:2J3H"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:2J3H"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:2J3H"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:2J3H"
FT HELIX 273..277
FT /evidence="ECO:0007829|PDB:2J3H"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:2J3H"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:2J3H"
FT HELIX 293..305
FT /evidence="ECO:0007829|PDB:2J3H"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:2J3H"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:2J3H"
FT HELIX 323..330
FT /evidence="ECO:0007829|PDB:2J3H"
FT STRAND 335..343
FT /evidence="ECO:0007829|PDB:2J3H"
SQ SEQUENCE 345 AA; 38134 MW; 5AFCEBB2948B2680 CRC64;
MTATNKQVIL KDYVSGFPTE SDFDFTTTTV ELRVPEGTNS VLVKNLYLSC DPYMRIRMGK
PDPSTAALAQ AYTPGQPIQG YGVSRIIESG HPDYKKGDLL WGIVAWEEYS VITPMTHAHF
KIQHTDVPLS YYTGLLGMPG MTAYAGFYEV CSPKEGETVY VSAASGAVGQ LVGQLAKMMG
CYVVGSAGSK EKVDLLKTKF GFDDAFNYKE ESDLTAALKR CFPNGIDIYF ENVGGKMLDA
VLVNMNMHGR IAVCGMISQY NLENQEGVHN LSNIIYKRIR IQGFVVSDFY DKYSKFLEFV
LPHIREGKIT YVEDVADGLE KAPEALVGLF HGKNVGKQVV VVARE
//
