TRNH1_ARATH
ID TRNH1_ARATH Reviewed; 266 AA.
AC P0DKI3; Q9ASX2; Q9LNW5;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Tropinone reductase homolog At1g07440 {ECO:0000305};
DE EC=1.1.1.- {ECO:0000305};
GN OrderedLocusNames=At1g07440 {ECO:0000312|Araport:AT1G07440};
GN ORFNames=F22G5.16, F22G5.20 {ECO:0000312|EMBL:AAF79553.1}, F22G5.39;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 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 X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RG Center for eukaryotic structural genomics (CESG);
RT "X-ray structure of putative tropinone reductase from Arabidopsis thaliana
RT At1g07440.";
RL Submitted (FEB-2005) to the PDB data bank.
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=P0DKI3-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. SDR65C subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79553.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At1g07440 and At1g07450.; Evidence={ECO:0000305};
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DR EMBL; AC022464; AAF79553.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28125.1; -; Genomic_DNA.
DR EMBL; AF361621; AAK32789.1; -; mRNA.
DR EMBL; AY055094; AAL05894.1; -; mRNA.
DR PIR; C86209; C86209.
DR RefSeq; NP_172224.1; NM_100618.5. [P0DKI3-1]
DR PDB; 1XQ1; X-ray; 2.10 A; A=1-266.
DR PDB; 2Q45; X-ray; 2.10 A; A=1-266.
DR PDBsum; 1XQ1; -.
DR PDBsum; 2Q45; -.
DR AlphaFoldDB; P0DKI3; -.
DR SMR; P0DKI3; -.
DR STRING; 3702.AT1G07440.1; -.
DR PaxDb; P0DKI3; -.
DR PRIDE; P0DKI3; -.
DR ProteomicsDB; 242801; -. [P0DKI3-1]
DR DNASU; 837256; -.
DR EnsemblPlants; AT1G07440.1; AT1G07440.1; AT1G07440. [P0DKI3-1]
DR GeneID; 837256; -.
DR Gramene; AT1G07440.1; AT1G07440.1; AT1G07440. [P0DKI3-1]
DR KEGG; ath:AT1G07440; -.
DR Araport; AT1G07440; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_1_1; -.
DR OMA; VPYHEYT; -.
DR PhylomeDB; P0DKI3; -.
DR PRO; PR:P0DKI3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P0DKI3; baseline and differential.
DR Genevisible; P0DKI3; 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 3D-structure; Alternative splicing; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..266
FT /note="Tropinone reductase homolog At1g07440"
FT /id="PRO_0000054789"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 18..42
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P50162"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P50162"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:2Q45"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1XQ1"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:1XQ1"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:1XQ1"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1XQ1"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:1XQ1"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1XQ1"
FT HELIX 75..89
FT /evidence="ECO:0007829|PDB:1XQ1"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1XQ1"
FT HELIX 113..141
FT /evidence="ECO:0007829|PDB:1XQ1"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:1XQ1"
FT HELIX 163..182
FT /evidence="ECO:0007829|PDB:1XQ1"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1XQ1"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:1XQ1"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:1XQ1"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:1XQ1"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:1XQ1"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:1XQ1"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:1XQ1"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:1XQ1"
SQ SEQUENCE 266 AA; 28332 MW; 45F0CEE052D37559 CRC64;
MAGAEQSQRW SLKAKTVLVT GGTKGIGHAI VEEFAGFGAV IHTCARNEYE LNECLSKWQK
KGFQVTGSVC DASLRPEREK LMQTVSSMFG GKLDILINNL GAIRSKPTLD YTAEDFSFHI
STNLESAYHL SQLAHPLLKA SGCGNIIFMS SIAGVVSASV GSIYSATKGA LNQLARNLAC
EWASDGIRAN AVAPAVIATP LAEAVYDDEF KKVVISRKPL GRFGEPEEVS SLVAFLCMPA
ASYITGQTIC VDGGLTVNGF SYQPQG
