TRNHC_ARATH
ID TRNHC_ARATH Reviewed; 271 AA.
AC Q9ZW19; Q8LCG4;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Tropinone reductase homolog At2g29360 {ECO:0000305};
DE EC=1.1.1.- {ECO:0000305};
GN Name=SDR {ECO:0000303|PubMed:18221363};
GN OrderedLocusNames=At2g29360 {ECO:0000312|Araport:AT2G29360};
GN ORFNames=F16P2.26 {ECO:0000312|EMBL:AAC95202.1};
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;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, AND
RP MUTAGENESIS OF SER-209.
RC STRAIN=cv. Columbia;
RX PubMed=18221363; DOI=10.1111/j.1365-313x.2008.03422.x;
RA Brock A., Brandt W., Drager B.;
RT "The functional divergence of short-chain dehydrogenases involved in
RT tropinone reduction.";
RL Plant J. 54:388-401(2008).
RN [6]
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).
CC -!- FUNCTION: Oxidoreductase active on cyclic ketones, but not on tropinone
CC or nortropinone. {ECO:0000269|PubMed:18221363}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.16 mM for quinuclidinone {ECO:0000269|PubMed:18221363};
CC KM=0.30 mM for 4-methylcyclohexanone {ECO:0000269|PubMed:18221363};
CC Vmax=6.63 nmol/sec/mg enzyme with quinuclidinone as substrate
CC {ECO:0000269|PubMed:18221363};
CC Vmax=105.63 nmol/sec/mg enzyme with 4-methylcyclohexanone as
CC substrate {ECO:0000269|PubMed:18221363};
CC pH dependence:
CC Optimum pH is 7.5 for quinuclidinone reduction. Optimum pH is 6.0 for
CC 4-methylcyclohexanone reduction. {ECO:0000269|PubMed:18221363};
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. SDR65C subfamily. {ECO:0000305}.
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DR EMBL; AC004561; AAC95202.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08242.1; -; Genomic_DNA.
DR EMBL; AY045613; AAK73971.1; -; mRNA.
DR EMBL; AY090333; AAL90994.1; -; mRNA.
DR EMBL; AY086609; AAM63669.1; -; mRNA.
DR PIR; D84695; D84695.
DR RefSeq; NP_180497.1; NM_128490.4.
DR AlphaFoldDB; Q9ZW19; -.
DR SMR; Q9ZW19; -.
DR IntAct; Q9ZW19; 2.
DR STRING; 3702.AT2G29360.1; -.
DR PaxDb; Q9ZW19; -.
DR PRIDE; Q9ZW19; -.
DR ProteomicsDB; 232409; -.
DR EnsemblPlants; AT2G29360.1; AT2G29360.1; AT2G29360.
DR GeneID; 817485; -.
DR Gramene; AT2G29360.1; AT2G29360.1; AT2G29360.
DR KEGG; ath:AT2G29360; -.
DR Araport; AT2G29360; -.
DR TAIR; locus:2043167; AT2G29360.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; Q9ZW19; -.
DR OMA; ANCINGC; -.
DR OrthoDB; 1194344at2759; -.
DR PhylomeDB; Q9ZW19; -.
DR BioCyc; ARA:AT2G29360-MON; -.
DR SABIO-RK; Q9ZW19; -.
DR PRO; PR:Q9ZW19; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW19; baseline and differential.
DR Genevisible; Q9ZW19; AT.
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..271
FT /note="Tropinone reductase homolog At2g29360"
FT /id="PRO_0000432367"
FT ACT_SITE 168
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"
FT MUTAGEN 209
FT /note="S->Y: Loss of activity with quinuclidinone and
FT decreased activity with cyclohexanones."
FT /evidence="ECO:0000269|PubMed:18221363"
FT CONFLICT 259
FT /note="G -> V (in Ref. 4; AAM63669)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 29185 MW; 48203BFE26699617 CRC64;
MAKTGESLRD KPRWSLVGMT ALVTGGSKGI GEAVVEELAT LGARIHTCAR DETQLQESLR
KWQAKGFQVT TSVCDVSSRD KREKLMETVS TIFEGKLNIL VNNVGTCIVK PTLQHTAEDF
SFTMATNLES AFHLSQLAHP LLKASGSGSI VLISSVSGVV HVNGASIYGV SKGAMNQLGR
NLACEWASDN IRTNSVCPWF IETPLVTESL SNEEFRKEVE SRPPMGRVGE VNEVSSLVAF
LCLPAASYIT GQTICVDGGF TVNGFSFKPL P
