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TRNH5_ARATH
ID   TRNH5_ARATH             Reviewed;         322 AA.
AC   Q9ZW12; Q84W78;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Tropinone reductase homolog At2g29260, chloroplastic {ECO:0000305};
DE            EC=1.1.1.- {ECO:0000305};
DE   Flags: Precursor;
GN   OrderedLocusNames=At2g29260 {ECO:0000312|Araport:AT2G29260};
GN   ORFNames=F16P2.36 {ECO:0000312|EMBL:AAC95209.1};
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 11-322.
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. SDR65C subfamily. {ECO:0000305}.
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DR   EMBL; AC004561; AAC95209.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08226.1; -; Genomic_DNA.
DR   EMBL; BT004138; AAO42159.1; -; mRNA.
DR   PIR; D84694; D84694.
DR   RefSeq; NP_180489.1; NM_128482.4.
DR   AlphaFoldDB; Q9ZW12; -.
DR   SMR; Q9ZW12; -.
DR   STRING; 3702.AT2G29260.1; -.
DR   PaxDb; Q9ZW12; -.
DR   PRIDE; Q9ZW12; -.
DR   ProteomicsDB; 232407; -.
DR   EnsemblPlants; AT2G29260.1; AT2G29260.1; AT2G29260.
DR   GeneID; 817475; -.
DR   Gramene; AT2G29260.1; AT2G29260.1; AT2G29260.
DR   KEGG; ath:AT2G29260; -.
DR   Araport; AT2G29260; -.
DR   TAIR; locus:2043087; AT2G29260.
DR   eggNOG; KOG0725; Eukaryota.
DR   HOGENOM; CLU_010194_1_1_1; -.
DR   InParanoid; Q9ZW12; -.
DR   OMA; TWGGPFD; -.
DR   OrthoDB; 1194344at2759; -.
DR   PhylomeDB; Q9ZW12; -.
DR   BioCyc; ARA:AT2G29260-MON; -.
DR   PRO; PR:Q9ZW12; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZW12; baseline and differential.
DR   Genevisible; Q9ZW12; AT.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   Chloroplast; NADP; Oxidoreductase; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..61
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           62..322
FT                   /note="Tropinone reductase homolog At2g29260,
FT                   chloroplastic"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000432360"
FT   BINDING         74..98
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P50162"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P50162"
FT   CONFLICT        151
FT                   /note="I -> T (in Ref. 3; AAO42159)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   322 AA;  35238 MW;  2AF32C812B327789 CRC64;
     MVLDMASHLY TNPPQNLHFI SSSSSLKPHL CLSFKRINPK HKSSSSSVFV PYASQSSIAI
     TSKERWSLNG MSALVTGGTR GIGRAIVEEL AGLGAEVHTC ARNEYELENC LSDWNRSGFR
     VAGSVCDVSD RSQREALMET VSSVFEGKLH ILVNNVGTNI RKPMVEFTAG EFSTLMSTNF
     ESVFHLCQLA YPLLRESKAG SVVFISSVSG FVSLKNMSVQ SSTKGAINQL TRSLACEWAK
     DNIRINAVAP WYIKTSMVEQ VLSNKEYLEE VYSVTPLGRL GEPREVSSAV AFLCLPASSY
     ITGQILCVDG GMSINGFFPR HD
 
 
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