ID   TRXY_ORYSJ              Reviewed;         168 AA.
AC   Q5JMR9; Q0JFS8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Thioredoxin Y, chloroplastic;
DE            Short=OsTrxy;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os01g0963400, LOC_Os01g73234; ORFNames=P0483G10.36;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19825616; DOI=10.1093/mp/ssn076;
RA   Chibani K., Wingsle G., Jacquot J.P., Gelhaye E., Rouhier N.;
RT   "Comparative genomic study of the thioredoxin family in photosynthetic
RT   organisms with emphasis on Populus trichocarpa.";
RL   Mol. Plant 2:308-322(2009).
CC   -!- FUNCTION: Probable thiol-disulfide oxidoreductase that may participate
CC       in various redox reactions.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. Plant Y-type subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD87235.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF07400.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP003263; BAD87235.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008207; BAF07400.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015622279.1; XM_015766793.1.
DR   RefSeq; XP_015622287.1; XM_015766801.1.
DR   AlphaFoldDB; Q5JMR9; -.
DR   SMR; Q5JMR9; -.
DR   STRING; 4530.OS01T0963400-01; -.
DR   PaxDb; Q5JMR9; -.
DR   PRIDE; Q5JMR9; -.
DR   GeneID; 4324458; -.
DR   KEGG; osa:4324458; -.
DR   eggNOG; KOG0910; Eukaryota.
DR   HOGENOM; CLU_090389_10_4_1; -.
DR   InParanoid; Q5JMR9; -.
DR   OrthoDB; 1482186at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   Genevisible; Q5JMR9; OS.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IBA:GO_Central.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01068; thioredoxin; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Disulfide bond; Electron transport; Plastid;
KW   Redox-active center; Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..58
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           59..168
FT                   /note="Thioredoxin Y, chloroplastic"
FT                   /id="PRO_0000394836"
FT   DOMAIN          59..165
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        89
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        92
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            83
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            90
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            91
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        89..92
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   168 AA;  18181 MW;  58E3161C16599357 CRC64;
     MAAFTSTTTA AAASPTPCRP AALVARSSAA PLRSAAPVVV AAGLRRAAAP SRRGATLRVQ
     AKKQTFSSFD ELLEKSEKPV LVDFYATWCG PCQYMVPILQ EVSEKLGDKI QVVKIDTEKY
     TSIANRYQIE ALPTFIIFKN GKPCHRFEGA LPANQLIQQI ESALEVAK