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TRNH8_ARATH
ID   TRNH8_ARATH             Reviewed;         262 AA.
AC   Q9ZW14;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Tropinone reductase homolog At2g29310 {ECO:0000305};
DE            EC=1.1.1.- {ECO:0000305};
GN   OrderedLocusNames=At2g29310 {ECO:0000312|Araport:AT2G29310};
GN   ORFNames=F16P2.31 {ECO:0000312|EMBL:AAC95207.1};
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 (SEP-2004) 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).
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=Q9ZW14-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. SDR65C subfamily. {ECO:0000305}.
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DR   EMBL; AC004561; AAC95207.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08232.1; -; Genomic_DNA.
DR   EMBL; BT010425; AAQ62426.1; -; mRNA.
DR   EMBL; AK175221; BAD42984.1; -; mRNA.
DR   PIR; G84694; G84694.
DR   RefSeq; NP_180492.1; NM_128485.4. [Q9ZW14-1]
DR   AlphaFoldDB; Q9ZW14; -.
DR   SMR; Q9ZW14; -.
DR   IntAct; Q9ZW14; 5.
DR   STRING; 3702.AT2G29310.1; -.
DR   PaxDb; Q9ZW14; -.
DR   PRIDE; Q9ZW14; -.
DR   ProteomicsDB; 232444; -. [Q9ZW14-1]
DR   EnsemblPlants; AT2G29310.1; AT2G29310.1; AT2G29310. [Q9ZW14-1]
DR   GeneID; 817480; -.
DR   Gramene; AT2G29310.1; AT2G29310.1; AT2G29310. [Q9ZW14-1]
DR   KEGG; ath:AT2G29310; -.
DR   Araport; AT2G29310; -.
DR   TAIR; locus:2043027; AT2G29310.
DR   eggNOG; KOG0725; Eukaryota.
DR   HOGENOM; CLU_010194_1_1_1; -.
DR   InParanoid; Q9ZW14; -.
DR   OMA; PFTEHTA; -.
DR   OrthoDB; 1116724at2759; -.
DR   PhylomeDB; Q9ZW14; -.
DR   BioCyc; ARA:AT2G29310-MON; -.
DR   PRO; PR:Q9ZW14; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZW14; baseline and differential.
DR   Genevisible; Q9ZW14; 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   2: Evidence at transcript level;
KW   Alternative splicing; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..262
FT                   /note="Tropinone reductase homolog At2g29310"
FT                   /id="PRO_0000432363"
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   262 AA;  28089 MW;  4F0B06604CA00A07 CRC64;
     MDKRWSLQGM TALVTGAASG IGYAIVEELA SFGAIIHICD ISETLLSQSL SEWEKKGFQV
     SGSICDVASR PDREKLMQTV SSLFDGKLNI LVNNVGVIRG KPTTEYVAED FSYHISTNLE
     PAFHFSQLSH LLLKASGFGS IVFMSSATGV VSVQCGSIYS LTKGALNQLT RNLACEWAKD
     GIRANAVAPN VVKTPLSQSY LEDVGFKEAL FSRTPLGRAG EPNEVASLVV FLCLPAASYI
     TGQTICIDGG FTVNAFSYKP QA
 
 
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