SDR1_ARATH
ID SDR1_ARATH Reviewed; 296 AA.
AC Q9M2E2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=(+)-neomenthol dehydrogenase {ECO:0000303|PubMed:18599651};
DE EC=1.1.1.- {ECO:0000269|PubMed:21169366};
DE EC=1.1.1.208 {ECO:0000269|PubMed:18599651};
DE AltName: Full=Menthone:neomenthol reductase;
DE AltName: Full=Short-chain dehydrogenase/reductase 1;
DE Short=AtSDR1;
GN Name=SDR1; OrderedLocusNames=At3g61220 {ECO:0000312|Araport:AT3G61220};
GN ORFNames=T20K12.120 {ECO:0000312|EMBL:CAB71052.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=18599651; DOI=10.1104/pp.108.119461;
RA Choi H.W., Lee B.G., Kim N.H., Park Y., Lim C.W., Song H.K., Hwang B.K.;
RT "A role for a menthone reductase in resistance against microbial pathogens
RT in plants.";
RL Plant Physiol. 148:383-401(2008).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21169366; DOI=10.1074/jbc.m110.202226;
RA Yamauchi Y., Hasegawa A., Taninaka A., Mizutani M., Sugimoto Y.;
RT "NADPH-dependent reductases involved in the detoxification of reactive
RT carbonyls in plants.";
RL J. Biol. Chem. 286:6999-7009(2011).
CC -!- FUNCTION: Aldehyde reductase that catalyzes the reduction of the
CC aldehyde carbonyl groups on saturated and alpha,beta-unsaturated
CC aldehydes with more than 5 carbons (PubMed:21169366). Involved in basal
CC resistance against pathogens. {ECO:0000269|PubMed:18599651,
CC ECO:0000269|PubMed:21169366}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-neomenthol + NADP(+) = (1R,4S)-menthone + H(+) + NADPH;
CC Xref=Rhea:RHEA:23812, ChEBI:CHEBI:15378, ChEBI:CHEBI:15402,
CC ChEBI:CHEBI:15410, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.208; Evidence={ECO:0000269|PubMed:18599651};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.07 mM for (E)-2-pentenal {ECO:0000269|PubMed:21169366};
CC KM=0.53 mM for (E)-2-hexenal {ECO:0000269|PubMed:21169366};
CC Note=kcat is 0.27 sec(-1) for (E)-2-pentenal. kcat is 0.4 sec(-1) for
CC (E)-2-hexenal. {ECO:0000269|PubMed:21169366};
CC pH dependence:
CC Optimum pH is 9.0 for the forward reaction and 8.0 for the reverse
CC reaction. {ECO:0000269|PubMed:18599651};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21169366}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M2E2-1; Sequence=Displayed;
CC -!- INDUCTION: By pathogen infection. Not detected in healthy leaves.
CC {ECO:0000269|PubMed:18599651}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AL137898; CAB71052.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80174.1; -; Genomic_DNA.
DR EMBL; AY045884; AAK76558.1; -; mRNA.
DR EMBL; AY091305; AAM14244.1; -; mRNA.
DR PIR; T47914; T47914.
DR RefSeq; NP_191681.1; NM_115986.4. [Q9M2E2-1]
DR AlphaFoldDB; Q9M2E2; -.
DR SMR; Q9M2E2; -.
DR BioGRID; 10608; 1.
DR IntAct; Q9M2E2; 1.
DR STRING; 3702.AT3G61220.2; -.
DR PaxDb; Q9M2E2; -.
DR PRIDE; Q9M2E2; -.
DR ProteomicsDB; 232781; -. [Q9M2E2-1]
DR EnsemblPlants; AT3G61220.1; AT3G61220.1; AT3G61220. [Q9M2E2-1]
DR GeneID; 825294; -.
DR Gramene; AT3G61220.1; AT3G61220.1; AT3G61220. [Q9M2E2-1]
DR KEGG; ath:AT3G61220; -.
DR Araport; AT3G61220; -.
DR eggNOG; KOG1208; Eukaryota.
DR HOGENOM; CLU_010194_9_0_1; -.
DR InParanoid; Q9M2E2; -.
DR OMA; NIDYKAY; -.
DR PhylomeDB; Q9M2E2; -.
DR BioCyc; ARA:AT3G61220-MON; -.
DR BioCyc; MetaCyc:AT3G61220-MON; -.
DR BRENDA; 1.1.1.208; 399.
DR SABIO-RK; Q9M2E2; -.
DR PRO; PR:Q9M2E2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2E2; baseline and differential.
DR Genevisible; Q9M2E2; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047501; F:(+)-neomenthol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR CDD; cd05324; carb_red_PTCR-like_SDR_c; 1.
DR InterPro; IPR045313; CBR1-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; NADP; Oxidoreductase; Plant defense;
KW Reference proteome.
FT CHAIN 1..296
FT /note="(+)-neomenthol dehydrogenase"
FT /id="PRO_0000349098"
FT ACT_SITE 220
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q12634"
FT BINDING 16..40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q12634"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12634"
SQ SEQUENCE 296 AA; 32803 MW; 395A33A153E67A0D CRC64;
MAEETPRYAV VTGANRGIGF EICRQLASEG IRVVLTSRDE NRGLEAVETL KKELEISDQS
LLFHQLDVAD PASITSLAEF VKTQFGKLDI LVNNAGIGGI ITDAEALRAG AGKEGFKWDE
IITETYELTE ECIKINYYGP KRMCEAFIPL LKLSDSPRIV NVSSSMGQLK NVLNEWAKGI
LSDAENLTEE RIDQVINQLL NDFKEGTVKE KNWAKFMSAY VVSKASLNGY TRVLAKKHPE
FRVNAVCPGF VKTDMNFKTG VLSVEEGASS PVRLALLPHQ ETPSGCFFSR KQVSEF
