TRNH3_ARATH
ID TRNH3_ARATH Reviewed; 268 AA.
AC Q9ZW03;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Tropinone reductase homolog At2g29150 {ECO:0000305};
DE EC=1.1.1.- {ECO:0000305};
GN OrderedLocusNames=At2g29150 {ECO:0000312|Araport:AT2G29150};
GN ORFNames=F16P2.47 {ECO:0000312|EMBL:AAC95219.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19027726; DOI=10.1016/j.cbi.2008.10.040;
RA Persson B., Kallberg Y., Bray J.E., Bruford E., Dellaporta S.L.,
RA Favia A.D., Duarte R.G., Joernvall H., Kavanagh K.L., Kedishvili N.,
RA Kisiela M., Maser E., Mindnich R., Orchard S., Penning T.M., Thornton J.M.,
RA Adamski J., Oppermann U.;
RT "The SDR (short-chain dehydrogenase/reductase and related enzymes)
RT nomenclature initiative.";
RL Chem. Biol. Interact. 178:94-98(2009).
RN [5]
RP FUNCTION, 3D-STRUCTURE MODELING, SUBSTRATE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24583623; DOI=10.1016/j.bioorg.2014.01.004;
RA Reinhardt N., Fischer J., Coppi R., Blum E., Brandt W., Draeger B.;
RT "Substrate flexibility and reaction specificity of tropinone reductase-like
RT short-chain dehydrogenases.";
RL Bioorg. Chem. 53:37-49(2014).
CC -!- FUNCTION: Enantiospecific reductase active on cyclic monoterpenes and
CC small flexible lipophilic carbonyls. No activity with tropinone,
CC nitrogen-containing tropinone analogs, tropine or pseudotropine as
CC substrate. {ECO:0000269|PubMed:24583623}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.1 uM for NADPH {ECO:0000269|PubMed:24583623};
CC KM=4.8 uM for NADP {ECO:0000269|PubMed:24583623};
CC KM=74.5 uM for citronellal {ECO:0000269|PubMed:24583623};
CC KM=67.4 uM for nerol {ECO:0000269|PubMed:24583623};
CC KM=559.5 uM for 3-methylcyclohexanone {ECO:0000269|PubMed:24583623};
CC KM=315.2 uM for 3-methylcyclohexanol {ECO:0000269|PubMed:24583623};
CC KM=106.0 uM for 4-methylcyclohexanone {ECO:0000269|PubMed:24583623};
CC KM=378.5 uM for 4-methylcyclohexanol {ECO:0000269|PubMed:24583623};
CC KM=452.4 uM for (-)-menthone {ECO:0000269|PubMed:24583623};
CC KM=113.0 uM for (-)-neomenthol {ECO:0000269|PubMed:24583623};
CC KM=1830.0 uM for (-)-carvone {ECO:0000269|PubMed:24583623};
CC KM=891.5 uM for (-)-alpha-thujone {ECO:0000269|PubMed:24583623};
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. SDR65C subfamily. {ECO:0000305}.
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DR EMBL; AC004561; AAC95219.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08217.1; -; Genomic_DNA.
DR EMBL; DQ056552; AAY78703.1; -; mRNA.
DR PIR; B84693; B84693.
DR RefSeq; NP_180479.1; NM_128472.1.
DR AlphaFoldDB; Q9ZW03; -.
DR SMR; Q9ZW03; -.
DR STRING; 3702.AT2G29150.1; -.
DR iPTMnet; Q9ZW03; -.
DR PaxDb; Q9ZW03; -.
DR PRIDE; Q9ZW03; -.
DR ProteomicsDB; 232469; -.
DR EnsemblPlants; AT2G29150.1; AT2G29150.1; AT2G29150.
DR GeneID; 817464; -.
DR Gramene; AT2G29150.1; AT2G29150.1; AT2G29150.
DR KEGG; ath:AT2G29150; -.
DR Araport; AT2G29150; -.
DR TAIR; locus:2043037; AT2G29150.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; Q9ZW03; -.
DR OMA; VTEERCA; -.
DR OrthoDB; 1194344at2759; -.
DR PhylomeDB; Q9ZW03; -.
DR BioCyc; ARA:AT2G29150-MON; -.
DR SABIO-RK; Q9ZW03; -.
DR PRO; PR:Q9ZW03; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW03; baseline and differential.
DR Genevisible; Q9ZW03; AT.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR045000; TR.
DR PANTHER; PTHR42898; PTHR42898; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..268
FT /note="Tropinone reductase homolog At2g29150"
FT /id="PRO_0000432358"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 22..46
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P50162"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P50162"
SQ SEQUENCE 268 AA; 28706 MW; F236D9F6FA0E301C CRC64;
MAKAGENSRD KSRWSLEGMT ALVTGGSKGL GEAVVEELAM LGARVHTCAR DETQLQERLR
EWQAKGFEVT TSVCDVSSRE QREKLMETVS SVFQGKLNIL VNNAGTGIIK PSTEYTAEDY
SFLMATNLES AFHLSQIAHP LLKASGSGSI VFMSSVAGLV HTGASIYGAS KGAMNQLGRS
LACEWASDNI RVNSVCPWVI TTPLTSFIFS DEKLRKAVED KTPMGRVGEA NEVSSLVAFL
CFPAASYITG QTICVDGGAS VNGFSFKP
