P2_ARATH
ID P2_ARATH Reviewed; 343 AA.
AC Q39173; Q9LFK3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=NADP-dependent alkenal double bond reductase P2;
DE EC=1.3.1.74;
GN Name=P2; OrderedLocusNames=At5g16990; ORFNames=F2K13_140;
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].
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).
CC -!- FUNCTION: Catalyzes the reduction of the 7-8 double bond of
CC phenylpropanal substrates, such as p-coumaryl aldehyde and coniferyl
CC aldehyde (in vitro). Has activity towards toxic substrates, such as 4-
CC hydroxy-(2E)-nonenal (in vitro) (By similarity). May play a distinct
CC role in plant antioxidant defense and is possibly involved in
CC NAD(P)/NAD(P)h homeostasis. {ECO:0000250}.
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 -!- 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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z49268; CAA89262.1; -; mRNA.
DR EMBL; AL391141; CAC01712.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92367.1; -; Genomic_DNA.
DR EMBL; AY091320; AAM14259.1; -; mRNA.
DR EMBL; AY065253; AAL38729.1; -; mRNA.
DR PIR; S57612; S57612.
DR PIR; T51554; T51554.
DR RefSeq; NP_197201.1; NM_121705.4.
DR AlphaFoldDB; Q39173; -.
DR SMR; Q39173; -.
DR BioGRID; 16838; 2.
DR IntAct; Q39173; 1.
DR STRING; 3702.AT5G16990.1; -.
DR PaxDb; Q39173; -.
DR PRIDE; Q39173; -.
DR ProteomicsDB; 248809; -.
DR DNASU; 831562; -.
DR EnsemblPlants; AT5G16990.1; AT5G16990.1; AT5G16990.
DR GeneID; 831562; -.
DR Gramene; AT5G16990.1; AT5G16990.1; AT5G16990.
DR KEGG; ath:AT5G16990; -.
DR Araport; AT5G16990; -.
DR TAIR; locus:2148166; AT5G16990.
DR eggNOG; KOG1196; Eukaryota.
DR HOGENOM; CLU_026673_29_1_1; -.
DR InParanoid; Q39173; -.
DR OMA; KMEGSYV; -.
DR OrthoDB; 884151at2759; -.
DR PhylomeDB; Q39173; -.
DR BioCyc; ARA:AT5G16990-MON; -.
DR PRO; PR:Q39173; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39173; baseline and differential.
DR Genevisible; Q39173; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IEP: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 2: Evidence at transcript level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..343
FT /note="NADP-dependent alkenal double bond reductase P2"
FT /id="PRO_0000218074"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164..167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 252..258
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 282..284
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT CONFLICT 15
FT /note="Missing (in Ref. 1; CAA89262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 37989 MW; 491698EF58BA82DA CRC64;
MTTNKQVIFK DHVSGFPKES DFNFTTTTVE LRVPEGSKSV LVKNLYLSCD PYMRSRMGKP
DPSSALAQAY APGKPIYGYG VSRVIESGHP DYKKGDLLWG IVGWEEYSVI TPMAHMHFKI
QHTDVPLSYY TGLLGMPGMT AYAGFYEVCS PKKGETVYVS AASGAVGQLV GQFAKMMGCY
VVGSAGSKEK VDLLKTKFGF DDAFNYKEES DLSAALKRCF PKGIDMYFEN VGGKMLDAVL
LNMNPHGRIA VCGMISQYNL ENQEGVHNLS NIIYKRIRIQ GFVVADFYDK YPKFLELVLP
RIKEGKITYV EDVADGLEKA PEALVGLFHG KNVGKQVVVI ARE
