TRNHA_ARATH
ID TRNHA_ARATH Reviewed; 260 AA.
AC Q9ZW16;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Tropinone reductase homolog At2g29330 {ECO:0000305};
DE EC=1.1.1.- {ECO:0000305};
GN Name=TRI {ECO:0000312|EMBL:AEC08235.1};
GN OrderedLocusNames=At2g29330 {ECO:0000312|Araport:AT2G29330};
GN ORFNames=F16P2.29 {ECO:0000312|EMBL:AAC95205.1};
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP 3D-STRUCTURE MODELING, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND FUNCTION.
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: Reductase active only on small flexible lipophilic carbonyls.
CC No activity with cyclic monoterpenes, tropinone, nitrogen-containing
CC tropinone analogs, tropine or pseudotropine as substrate.
CC {ECO:0000269|PubMed:24583623}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=279.2 uM for NADPH {ECO:0000269|PubMed:24583623};
CC KM=59.3 uM for NADH {ECO:0000269|PubMed:24583623};
CC KM=15.0 uM for NAD {ECO:0000269|PubMed:24583623};
CC KM=108.7 uM for citronellal {ECO:0000269|PubMed:24583623};
CC KM=64.6 uM for pentanal {ECO:0000269|PubMed:24583623};
CC KM=389.7 uM for dimethylpentan-3-one {ECO:0000269|PubMed:24583623};
CC KM=464.1 uM for nerol {ECO:0000269|PubMed:24583623};
CC KM=56.7 uM for 3-methylcyclohexanone {ECO:0000269|PubMed:24583623};
CC KM=61.9 uM for 3-methylcyclohexanol {ECO:0000269|PubMed:24583623};
CC KM=71.5 uM for 4-methylcyclohexanone {ECO:0000269|PubMed:24583623};
CC KM=63.3 uM for 4-methylcyclohexanol {ECO:0000269|PubMed:24583623};
CC KM=105.6 uM for 1,4-cyclohexanedione {ECO:0000269|PubMed:24583623};
CC Note=kcat is 0.34 sec(-1) for NADH. kcat is 0.000003 sec(-1) for NAD.
CC {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; AAC95205.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08235.1; -; Genomic_DNA.
DR EMBL; BT005864; AAO64799.1; -; mRNA.
DR EMBL; AK227484; BAE99485.1; -; mRNA.
DR PIR; A84695; A84695.
DR RefSeq; NP_180494.1; NM_128487.3.
DR AlphaFoldDB; Q9ZW16; -.
DR SMR; Q9ZW16; -.
DR IntAct; Q9ZW16; 2.
DR STRING; 3702.AT2G29330.1; -.
DR PaxDb; Q9ZW16; -.
DR PRIDE; Q9ZW16; -.
DR ProteomicsDB; 228724; -.
DR EnsemblPlants; AT2G29330.1; AT2G29330.1; AT2G29330.
DR GeneID; 817482; -.
DR Gramene; AT2G29330.1; AT2G29330.1; AT2G29330.
DR KEGG; ath:AT2G29330; -.
DR Araport; AT2G29330; -.
DR TAIR; locus:2042992; AT2G29330.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; Q9ZW16; -.
DR OMA; GANVMFA; -.
DR OrthoDB; 1194344at2759; -.
DR PhylomeDB; Q9ZW16; -.
DR BioCyc; ARA:AT2G29330-MON; -.
DR SABIO-RK; Q9ZW16; -.
DR PRO; PR:Q9ZW16; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW16; baseline and differential.
DR Genevisible; Q9ZW16; 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; 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.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..260
FT /note="Tropinone reductase homolog At2g29330"
FT /id="PRO_0000432365"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 13..37
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P50162"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P50162"
SQ SEQUENCE 260 AA; 27662 MW; C468ED940B3C9173 CRC64;
MDKRWSLQGL TALVTGGASG IGHAIVEELA GFGAKIHVCD ISKTLLNQSL SEWEKKGFQV
SGSVCDASNR LERETLMQTV TTIFDGKLNI LVNNVGTIRT KPTIEYEAED FSFLISTNLE
SAYHLSQLSH PLLKASGNGI ITFISSAAGI VSFDAASIYG LTKGALNQLA RNLACEWAKD
GIRANAVAPN FITTALAKPF LEDAGFNEIL SSRTPLGRAG EPREVASLVA FLCLPAASYI
TGQTICVDGG LTVNGFSYQP
