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TRNH9_ARATH
ID   TRNH9_ARATH             Reviewed;         269 AA.
AC   Q9ZW15; Q941D2;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Tropinone reductase homolog At2g29320 {ECO:0000305};
DE            EC=1.1.1.- {ECO:0000305};
GN   OrderedLocusNames=At2g29320 {ECO:0000312|Araport:AT2G29320};
GN   ORFNames=F16P2.30 {ECO:0000312|EMBL:AAC95206.1};
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] OF 3-269.
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   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   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. SDR65C subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK97712.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC004561; AAC95206.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08234.1; -; Genomic_DNA.
DR   EMBL; AY052242; AAK97712.1; ALT_INIT; mRNA.
DR   EMBL; BT001027; AAN46781.1; -; mRNA.
DR   PIR; H84694; H84694.
DR   RefSeq; NP_180493.1; NM_128486.3.
DR   AlphaFoldDB; Q9ZW15; -.
DR   SMR; Q9ZW15; -.
DR   IntAct; Q9ZW15; 4.
DR   STRING; 3702.AT2G29320.1; -.
DR   PaxDb; Q9ZW15; -.
DR   PRIDE; Q9ZW15; -.
DR   ProteomicsDB; 232381; -.
DR   EnsemblPlants; AT2G29320.1; AT2G29320.1; AT2G29320.
DR   GeneID; 817481; -.
DR   Gramene; AT2G29320.1; AT2G29320.1; AT2G29320.
DR   KEGG; ath:AT2G29320; -.
DR   Araport; AT2G29320; -.
DR   TAIR; locus:2043012; AT2G29320.
DR   eggNOG; KOG0725; Eukaryota.
DR   HOGENOM; CLU_010194_1_1_1; -.
DR   InParanoid; Q9ZW15; -.
DR   OMA; FHETAKD; -.
DR   OrthoDB; 1116724at2759; -.
DR   PhylomeDB; Q9ZW15; -.
DR   BioCyc; ARA:AT2G29320-MON; -.
DR   PRO; PR:Q9ZW15; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZW15; baseline and differential.
DR   Genevisible; Q9ZW15; AT.
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   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..269
FT                   /note="Tropinone reductase homolog At2g29320"
FT                   /id="PRO_0000432364"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         19..43
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P50162"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P50162"
SQ   SEQUENCE   269 AA;  28777 MW;  1405194EEEC8688F CRC64;
     MVTRKMDKRL WSLQGMTALV TGAASGIGYA IVEELAGFGA KIHICDISKT LLNQSLSEWE
     NKGFQVSGSV CDVTSHPERE KLMQTVSSIF DGKLNILVNN VGVLRGKPTT EYVADDFTFH
     ISTNLEAAYH FCQLSHPLLK ASGYGSIVFL SSVAGVVSLI DCGSIYGLTK GALNQLARNL
     ACEWAKDGIR ANAVAPNVVK TAQSQSFLED VSKKEGLLSR TPLGRVGEPN EVSSLVVFLC
     LPAASYITGQ TICVDGGLTV NGFSYQPHA
 
 
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