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AER_ARATH
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   03-AUG-2022, entry version 149.
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.AT5G16970.1; -.
DR   iPTMnet; Q39172; -.
DR   PaxDb; Q39172; -.
DR   PRIDE; Q39172; -.
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; locus:2148131; AT5G16970.
DR   eggNOG; KOG1196; Eukaryota.
DR   HOGENOM; CLU_026673_29_1_1; -.
DR   InParanoid; Q39172; -.
DR   OMA; GEVITNC; -.
DR   OrthoDB; 884151at2759; -.
DR   PhylomeDB; Q39172; -.
DR   BioCyc; ARA:AT5G16970-MON; -.
DR   BioCyc; MetaCyc:AT5G16970-MON; -.
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   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; PTHR43205; 1.
DR   Pfam; PF16884; ADH_N_2; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 2.
DR   SUPFAM; SSF51735; SSF51735; 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
 
 
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