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NADPH-dependent oxidoreductase 2-alkenal reductase (AtAER) (EC 1.3.1.-) (EC 1.3.1.74) (NADP-dependent alkenal double bond reductase P1) (DBR1) (NADPH-azodicarbonyl/quinone reductase) (NADPH:2-alkenal/one alpha,beta-hydrogenase) (ALH) (P1-zeta-crystallin protein) (P1-ZCr)

 AER_ARATH               Reviewed;         345 AA.
Q39172; Q501A9; Q8L865;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-APR-2018, entry version 129.
RecName: Full=NADPH-dependent oxidoreductase 2-alkenal reductase {ECO:0000303|PubMed:16299173};
Short=AtAER {ECO:0000303|PubMed:16299173};
EC=1.3.1.- {ECO:0000269|PubMed:10848984};
EC=1.3.1.74 {ECO:0000269|PubMed:12514241, ECO:0000269|PubMed:16299173, ECO:0000269|PubMed:17028190, ECO:0000269|PubMed:26678323};
AltName: Full=NADP-dependent alkenal double bond reductase P1 {ECO:0000303|PubMed:17028190};
Short=DBR1 {ECO:0000303|PubMed:17028190};
AltName: Full=NADPH-azodicarbonyl/quinone reductase {ECO:0000303|PubMed:10848984};
AltName: Full=NADPH:2-alkenal/one alpha,beta-hydrogenase {ECO:0000303|PubMed:12514241};
Short=ALH {ECO:0000303|PubMed:12514241};
AltName: Full=P1-zeta-crystallin protein {ECO:0000303|PubMed:7592828};
Short=P1-ZCr {ECO:0000303|PubMed:7592828};
Name=AER {ECO:0000303|PubMed:16299173};
Synonyms=P1 {ECO:0000303|PubMed:7592828};
OrderedLocusNames=At5g16970 {ECO:0000312|Araport:AT5G16970};
ORFNames=F2K13_120 {ECO:0000312|EMBL:CAC01710.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY OXIDATIVE STRESS.
STRAIN=cv. Columbia;
PubMed=7592828; DOI=10.1074/jbc.270.44.26224;
Babiychuk E., Kushnir S., Belles-Boix E., van Montagu M., Inze D.;
"Arabidopsis thaliana NADPH oxidoreductase homologs confer tolerance
of yeasts toward the thiol-oxidizing drug diamide.";
J. Biol. Chem. 270:26224-26231(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
AND ENZYME REGULATION.
PubMed=10848984; DOI=10.1046/j.1432-1327.2000.01398.x;
Mano J., Babiychuk E., Belles-Boix E., Hiratake J., Kimura A.,
Inze D., Kushnir S., Asada K.;
"A novel NADPH:diamide oxidoreductase activity in arabidopsis thaliana
P1 zeta-crystallin.";
Eur. J. Biochem. 267:3661-3671(2000).
[7]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12514241; DOI=10.1093/pcp/pcf187;
Mano J., Torii Y., Hayashi S., Takimoto K., Matsui K., Nakamura K.,
Inze D., Babiychuk E., Kushnir S., Asada K.;
"The NADPH:quinone oxidoreductase P1-zeta-crystallin in Arabidopsis
catalyzes the alpha,beta-hydrogenation of 2-alkenals: detoxication of
the lipid peroxide-derived reactive aldehydes.";
Plant Cell Physiol. 43:1445-1455(2002).
[8]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND TISSUE SPECIFICITY.
PubMed=16299173; DOI=10.1104/pp.105.070391;
Mano J., Belles-Boix E., Babiychuk E., Inze D., Torii Y., Hiraoka E.,
Takimoto K., Slooten L., Asada K., Kushnir S.;
"Protection against photooxidative injury of tobacco leaves by 2-
alkenal reductase. Detoxication of lipid peroxide-derived reactive
carbonyls.";
Plant Physiol. 139:1773-1783(2005).
[9]
CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=26678323; DOI=10.1016/j.phytochem.2015.11.015;
Curien G., Giustini C., Montillet J.L., Mas-Y-Mas S., Cobessi D.,
Ferrer J.L., Matringe M., Grechkin A., Rolland N.;
"The chloroplast membrane associated ceQORH putative quinone
oxidoreductase reduces long-chain, stress-related oxidized lipids.";
Phytochemistry 122:45-55(2016).
[10]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES AND
NADP, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBUNIT.
PubMed=17028190; DOI=10.1074/jbc.M605900200;
Youn B., Kim S.J., Moinuddin S.G., Lee C., Bedgar D.L., Harper A.R.,
Davin L.B., Lewis N.G., Kang C.;
"Mechanistic and structural studies of apoform, binary, and ternary
complexes of the Arabidopsis alkenal double bond reductase
At5g16970.";
J. Biol. Chem. 281:40076-40088(2006).
-!- FUNCTION: Involved in the detoxification of reactive carbonyls
(PubMed:10848984, PubMed:12514241, PubMed:16299173). Acts on lipid
peroxide-derived reactive aldehydes (PubMed:12514241). Specific to
a double bond activated by an adjacent carbonyl group
(PubMed:12514241). Can use both quinones and diamide as
substrates, but not menadione, ferricyanide or phylloquinone
(PubMed:10848984). Can use 4-hydroxy-(2E)-nonenal (HNE), 4-
hydroxy-(2E)-hexenal (HHE), (2E)-nonenal, (2E)-hexenal, (2E)-
pentenal, propenal (acrolein), 3-buten-2-one and 3-penten-2-one,
but not (R)-(-)-carvone, n-nonanal, n-hexanal, (3Z)-hexanal,
cyclohex-2-en-1-one or 12-oxo phytodienoic acid (OPDA) as electron
acceptors (PubMed:12514241). Catalyzes the reduction of the
alpha,beta-unsaturated bond of 2-alkenals, of lipid peroxide-
derived oxenes 9-oxo-10(E),12(Z)-octadecadienoic acid (9-KODE) and
13-oxo-9(Z),11(E)-octadecadienoic acid (13-KODE), as well as 4-
oxo-(2E)-nonenal and 4-hydroxynonenal (PubMed:16299173). Can use
12-oxo-10(E) dodecanoate (traumatin), trans-1,3 diphenyl-2-
propenone, trans-1,4-diphenyl-2-butene-1,4-dione, 9-oxo-12,13-
epoxy-(10E)-octadecenoic acid (trans-EKODE-1b) and 9,13-dihydroxy-
10-oxo-11-octadecenoic acid as substrates (PubMed:26678323).
Catalyzes the reduction of the 7-8 double bond of phenylpropanal
substrates, such as p-coumaryl aldehyde and coniferyl aldehyde (in
vitro) (PubMed:17028190). Has activity towards toxic substrates,
such as 4-hydroxy-(2E)-nonenal (in vitro) (PubMed:17028190). May
play a distinct role in plant antioxidant defense and is possibly
involved in NAD(P)/NAD(P)H homeostasis (PubMed:17028190).
{ECO:0000269|PubMed:10848984, ECO:0000269|PubMed:12514241,
ECO:0000269|PubMed:16299173, ECO:0000269|PubMed:17028190,
ECO:0000269|PubMed:26678323}.
-!- CATALYTIC ACTIVITY: A n-alkanal + NAD(P)(+) = an alk-2-enal +
NAD(P)H. {ECO:0000269|PubMed:12514241,
ECO:0000269|PubMed:16299173, ECO:0000269|PubMed:17028190,
ECO:0000269|PubMed:26678323}.
-!- ENZYME REGULATION: Inhibited by N-ethylmaleimide and p-
chloromercuribenzoic acid. {ECO:0000269|PubMed:10848984}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.53 mM for p-coumaryl aldehyde
{ECO:0000269|PubMed:17028190};
KM=0.41 mM for coniferyl aldehyde {ECO:0000269|PubMed:17028190};
KM=0.28 mM for 4-hydroxy-(2E)-nonenal
{ECO:0000269|PubMed:17028190};
KM=10 uM for trans-1,3 diphenyl-2-propenone
{ECO:0000269|PubMed:26678323};
KM=3.7 uM for trans-1,4-diphenyl-2-butene-1,4-dione
{ECO:0000269|PubMed:26678323};
KM=6.6 uM for traumatin {ECO:0000269|PubMed:26678323};
KM=0.65 uM for 9,10-phenanthrenequinone
{ECO:0000269|PubMed:10848984};
KM=11 uM for 5-Hydroxy-1,4-naphtoquinone
{ECO:0000269|PubMed:10848984};
KM=152 uM for 1,4-Benzoquinone {ECO:0000269|PubMed:10848984};
KM=25 uM for decyl-plastoquinone {ECO:0000269|PubMed:10848984};
KM=20 uM for ferricytochrome c {ECO:0000269|PubMed:10848984};
KM=128 uM for azodicarboxylic acid bis[dimethylamide]
{ECO:0000269|PubMed:10848984};
KM=120 uM for 1,10-(azocarbonyl)-dipeperidine
{ECO:0000269|PubMed:10848984};
KM=3.4 uM for azocarbonamide {ECO:0000269|PubMed:10848984};
KM=2.5 uM for NADPH for 9,10-phenanthrenequinone-reduction
{ECO:0000269|PubMed:10848984};
KM=8.2 uM for NADPH for azodicarboxylic acid bis[dimethylamide]-
reduction {ECO:0000269|PubMed:10848984};
KM=13.4 uM for 4-hydroxy-(2E)-nonenal
{ECO:0000269|PubMed:12514241};
KM=145 uM for 4-hydroxy-(2E)-hexenal
{ECO:0000269|PubMed:12514241};
KM=5.9 uM for (2E)-nonenal {ECO:0000269|PubMed:12514241};
KM=232 uM for (2E)-hexenal {ECO:0000269|PubMed:12514241};
KM=1420 uM for (2E)-pentenal {ECO:0000269|PubMed:12514241};
KM=4650 uM for propenal {ECO:0000269|PubMed:12514241};
KM=55 uM for 3-buten-2-one {ECO:0000269|PubMed:12514241};
KM=5.2 uM for 3-penten-2-one {ECO:0000269|PubMed:12514241};
KM=11.3 uM for (2E),(6Z)-nonadienal
{ECO:0000269|PubMed:16299173};
KM=1.24 uM for 4-oxo-(2E)-nonenal {ECO:0000269|PubMed:16299173};
KM=10.0 uM for 9-oxo-10(E),12(Z)-octadecadienoic acid
{ECO:0000269|PubMed:16299173};
KM=3.92 uM for 13-oxo-9(Z),11(E)-octadecadienoic acid
{ECO:0000269|PubMed:16299173};
KM=0.673 uM for 3-nonen-2-one {ECO:0000269|PubMed:16299173};
Note=kcat is 3.8 sec(-1) for trans-1,3 diphenyl-2-propenone.
kcat is 4.9 sec(-1) for trans-1,4-diphenyl-2-butene-1,4-dione.
kcat is 10 sec(-1) for traumatin (PubMed:26678323). kcat is 98
sec(-1) for 9,10-phenanthrenequinone. kcat is 1.9 sec(-1) for 5-
Hydroxy-1,4-naphtoquinone. kcat is 12 sec(-1) for 1,4-
Benzoquinone. kcat is 0.10 sec(-1) for decyl-plastoquinone. kcat
is 0.03 sec(-1) for ferricytochrome c. kcat is 95 sec(-1) for
azodicarboxylic acid bis[dimethylamide]. kcat is 42 sec(-1) for
1,10-(azocarbonyl)-dipeperidine. kcat is 31 sec(-1) for
azocarbonamide (PubMed:10848984). kcat is 88 sec(-1) for 4-
hydroxy-(2E)-nonenal. kcat is 42 sec(-1) for 4-hydroxy-(2E)-
hexenal. kcat is 51 sec(-1) for (2E)-nonenal. kcat is 63 sec(-1)
for (2E)-hexenal. kcat is 35 sec(-1) for (2E)-pentenal. kcat is
40 sec(-1) for propenal. kcat is 83 sec(-1) for 3-buten-2-one.
kcat is 103 sec(-1) for 3-penten-2-one (PubMed:12514241). kcat
is 33.9 sec(-1) for (2E),(6Z)-nonadienal. kcat is 20.1 sec(-1)
for 4-oxo-(2E)-nonenal. kcat is 0.94 sec(-1) for 9-oxo-
10(E),12(Z)-octadecadienoic acid. kcat is 1.10 sec(-1) for 13-
oxo-9(Z),11(E)-octadecadienoic acid. kcat is 18.9 sec(-1) for 3-
nonen-2-one (PubMed:16299173). {ECO:0000269|PubMed:10848984,
ECO:0000269|PubMed:12514241, ECO:0000269|PubMed:16299173,
ECO:0000269|PubMed:26678323};
pH dependence:
Optimum pH is 8.0 for 9,10-phenanthrenequinone-reduction.
Optimum pH is 6.5-7.0 for azodicarboxylic acid
bis[dimethylamide]-reduction (PubMed:10848984). Optimum pH is
6.0 with (2E)-hexenal or 4-hydroxy-(2E)-nonenal as substrate
(PubMed:12514241). {ECO:0000269|PubMed:10848984,
ECO:0000269|PubMed:12514241};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10848984,
ECO:0000269|PubMed:17028190}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16299173}.
Nucleus, nucleoplasm {ECO:0000269|PubMed:16299173}.
-!- TISSUE SPECIFICITY: Expressed in leaves.
{ECO:0000269|PubMed:16299173}.
-!- INDUCTION: Up-regulated upon treatment with paraquat, t-
butylhydroperoxide, diamide, and menadione.
{ECO:0000269|PubMed:7592828}.
-!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD
family. {ECO:0000305}.
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EMBL; Z49768; CAA89838.1; -; mRNA.
EMBL; AL391141; CAC01710.1; -; Genomic_DNA.
EMBL; CP002688; AED92364.1; -; Genomic_DNA.
EMBL; AY120718; AAM53276.1; -; mRNA.
EMBL; BT022058; AAY25470.1; -; mRNA.
PIR; S57611; S57611.
RefSeq; NP_197199.1; NM_121703.4.
UniGene; At.22432; -.
PDB; 2J3H; X-ray; 2.50 A; A/B=1-345.
PDB; 2J3I; X-ray; 2.80 A; A/B=1-345.
PDB; 2J3J; X-ray; 2.80 A; A/B=1-345.
PDB; 2J3K; X-ray; 2.80 A; A/B=1-345.
PDBsum; 2J3H; -.
PDBsum; 2J3I; -.
PDBsum; 2J3J; -.
PDBsum; 2J3K; -.
ProteinModelPortal; Q39172; -.
SMR; Q39172; -.
BioGrid; 16836; 2.
IntAct; Q39172; 1.
STRING; 3702.AT5G16970.1; -.
iPTMnet; Q39172; -.
PaxDb; Q39172; -.
PRIDE; Q39172; -.
DNASU; 831560; -.
EnsemblPlants; AT5G16970.1; AT5G16970.1; AT5G16970.
GeneID; 831560; -.
Gramene; AT5G16970.1; AT5G16970.1; AT5G16970.
KEGG; ath:AT5G16970; -.
Araport; AT5G16970; -.
TAIR; locus:2148131; AT5G16970.
eggNOG; KOG1196; Eukaryota.
eggNOG; COG2130; LUCA.
HOGENOM; HOG000294663; -.
InParanoid; Q39172; -.
KO; K08070; -.
OMA; IVAWEEY; -.
OrthoDB; EOG09360DUC; -.
PhylomeDB; Q39172; -.
BioCyc; ARA:AT5G16970-MONOMER; -.
BioCyc; MetaCyc:AT5G16970-MONOMER; -.
EvolutionaryTrace; Q39172; -.
PRO; PR:Q39172; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q39172; baseline and differential.
Genevisible; Q39172; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0032440; F:2-alkenal reductase [NAD(P)] activity; IDA:TAIR.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
InterPro; IPR013149; ADH_C.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020843; PKS_ER.
Pfam; PF00107; ADH_zinc_N; 1.
SMART; SM00829; PKS_ER; 1.
SUPFAM; SSF50129; SSF50129; 2.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; NADP; Nucleus;
Oxidoreductase; Reference proteome.
CHAIN 1 345 NADPH-dependent oxidoreductase 2-alkenal
reductase.
/FTId=PRO_0000218073.
NP_BIND 52 53 NADP. {ECO:0000244|PDB:2J3I}.
NP_BIND 163 169 NADP. {ECO:0000244|PDB:2J3I,
ECO:0000244|PDB:2J3J,
ECO:0000244|PDB:2J3K}.
NP_BIND 284 286 NADP. {ECO:0000244|PDB:2J3I,
ECO:0000244|PDB:2J3J,
ECO:0000244|PDB:2J3K}.
NP_BIND 334 336 NADP. {ECO:0000244|PDB:2J3I,
ECO:0000244|PDB:2J3J,
ECO:0000244|PDB:2J3K}.
BINDING 53 53 Substrate. {ECO:0000244|PDB:2J3K}.
BINDING 188 188 NADP; via amide nitrogen.
{ECO:0000244|PDB:2J3I,
ECO:0000244|PDB:2J3J,
ECO:0000244|PDB:2J3K}.
BINDING 192 192 NADP. {ECO:0000244|PDB:2J3I,
ECO:0000244|PDB:2J3J,
ECO:0000244|PDB:2J3K}.
BINDING 208 208 NADP. {ECO:0000244|PDB:2J3I,
ECO:0000244|PDB:2J3J,
ECO:0000244|PDB:2J3K}.
BINDING 232 232 NADP; via carbonyl oxygen.
{ECO:0000244|PDB:2J3J}.
BINDING 254 254 NADP. {ECO:0000244|PDB:2J3I,
ECO:0000244|PDB:2J3J,
ECO:0000244|PDB:2J3K}.
BINDING 260 260 NADP. {ECO:0000244|PDB:2J3I,
ECO:0000244|PDB:2J3J,
ECO:0000244|PDB:2J3K}.
BINDING 260 260 Substrate. {ECO:0000244|PDB:2J3K}.
BINDING 330 330 NADP; via carbonyl oxygen.
{ECO:0000244|PDB:2J3J,
ECO:0000244|PDB:2J3K}.
CONFLICT 223 223 P -> T (in Ref. 4; AAM53276).
{ECO:0000305}.
STRAND 2 10 {ECO:0000244|PDB:2J3H}.
STRAND 14 17 {ECO:0000244|PDB:2J3H}.
HELIX 20 22 {ECO:0000244|PDB:2J3H}.
STRAND 23 31 {ECO:0000244|PDB:2J3H}.
STRAND 36 39 {ECO:0000244|PDB:2J3H}.
STRAND 41 45 {ECO:0000244|PDB:2J3H}.
STRAND 47 49 {ECO:0000244|PDB:2J3H}.
HELIX 54 58 {ECO:0000244|PDB:2J3H}.
TURN 63 68 {ECO:0000244|PDB:2J3H}.
STRAND 79 89 {ECO:0000244|PDB:2J3H}.
STRAND 91 93 {ECO:0000244|PDB:2J3J}.
STRAND 99 112 {ECO:0000244|PDB:2J3H}.
TURN 116 118 {ECO:0000244|PDB:2J3H}.
STRAND 120 122 {ECO:0000244|PDB:2J3H}.
HELIX 131 133 {ECO:0000244|PDB:2J3H}.
TURN 134 136 {ECO:0000244|PDB:2J3H}.
HELIX 138 148 {ECO:0000244|PDB:2J3H}.
TURN 149 151 {ECO:0000244|PDB:2J3I}.
STRAND 158 163 {ECO:0000244|PDB:2J3H}.
HELIX 167 178 {ECO:0000244|PDB:2J3H}.
STRAND 182 189 {ECO:0000244|PDB:2J3H}.
HELIX 190 198 {ECO:0000244|PDB:2J3H}.
STRAND 203 207 {ECO:0000244|PDB:2J3H}.
HELIX 208 210 {ECO:0000244|PDB:2J3I}.
HELIX 215 221 {ECO:0000244|PDB:2J3H}.
STRAND 226 233 {ECO:0000244|PDB:2J3H}.
HELIX 235 242 {ECO:0000244|PDB:2J3H}.
STRAND 245 253 {ECO:0000244|PDB:2J3H}.
HELIX 257 259 {ECO:0000244|PDB:2J3H}.
HELIX 273 277 {ECO:0000244|PDB:2J3H}.
STRAND 280 283 {ECO:0000244|PDB:2J3H}.
HELIX 286 292 {ECO:0000244|PDB:2J3H}.
HELIX 293 305 {ECO:0000244|PDB:2J3H}.
STRAND 313 318 {ECO:0000244|PDB:2J3H}.
HELIX 319 321 {ECO:0000244|PDB:2J3H}.
HELIX 323 330 {ECO:0000244|PDB:2J3H}.
STRAND 335 343 {ECO:0000244|PDB:2J3H}.
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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