ID P1_ARATH Reviewed; 345 AA. AC Q39172; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 64. DE RecName: Full=Probable NADP-dependent oxidoreductase P1; DE EC=1.3.1.74; GN Name=P1; OrderedLocusNames=At5g16970; ORFNames=F2K13_120; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=96064691; 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 RT of 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 MEDLINE=21016721; 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., RA Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., RA Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., RA Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., RA Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., RA Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., RA Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., RA Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., RA Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., RA Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., RA Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., RA 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., RA Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., RA Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., RA van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., RA Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., RA Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., RA Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis RT thaliana."; RL Nature 408:823-826(2000). CC -!- FUNCTION: May play a distinct role in plant antioxidant defense CC and is possibly involved in NAD(P)/NAD(P)h homeostasis. CC -!- CATALYTIC ACTIVITY: n-alkanal + NAD(P)(+) = alk-2-enal + NAD(P)H. CC -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z49768; CAA89838.1; -; mRNA. DR EMBL; AL391141; CAC01710.1; -; Genomic_DNA. DR IPI; IPI00542017; -. DR PIR; S57611; S57611. DR RefSeq; NP_197199.1; -. DR UniGene; At.22432; -. 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 PRIDE; Q39172; -. DR ProMEX; Q39172; -. DR GeneID; 831560; -. DR GenomeReviews; BA000015_GR; AT5G16970. DR KEGG; ath:AT5G16970; -. DR TAIR; At5g16970; -. DR OMA; Q39172; MEGILAN. DR BRENDA; 1.3.1.74; 302. DR GermOnline; AT5G16970; Arabidopsis thaliana. DR GO; GO:0005829; C:cytosol; IDA:TAIR. DR GO; GO:0005634; C:nucleus; IDA:TAIR. DR GO; GO:0032440; F:2-alkenal reductase activity; IDA:TAIR. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR. DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR. DR InterPro; IPR002085; ADH_SF_Zn. DR InterPro; IPR013149; ADH_Zn-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR11695; ADH_Sf_Zn; 1. DR Pfam; PF00107; ADH_zinc_N; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; NADP; Oxidoreductase. FT CHAIN 1 345 Probable NADP-dependent oxidoreductase FT P1. FT /FTId=PRO_0000218073. FT STRAND 2 10 FT STRAND 14 17 FT HELIX 20 22 FT STRAND 23 31 FT STRAND 36 39 FT STRAND 41 45 FT STRAND 47 49 FT HELIX 54 58 FT STRAND 79 89 FT STRAND 99 112 FT TURN 116 118 FT STRAND 120 122 FT HELIX 131 133 FT TURN 134 136 FT HELIX 138 148 FT STRAND 158 163 FT HELIX 167 178 FT STRAND 182 189 FT HELIX 190 198 FT STRAND 203 207 FT HELIX 215 221 FT STRAND 226 233 FT HELIX 235 242 FT STRAND 245 253 FT HELIX 257 259 FT HELIX 273 277 FT STRAND 280 283 FT HELIX 286 292 FT HELIX 293 305 FT STRAND 313 318 FT HELIX 319 321 FT HELIX 323 330 FT STRAND 335 343 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 //