CITRX_ORYSI
ID CITRX_ORYSI Reviewed; 189 AA.
AC A2YUQ6;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Thioredoxin-like protein CITRX, chloroplastic {ECO:0000305};
DE EC=1.8.-.- {ECO:0000305};
DE AltName: Full=Cf-9-interacting thioredoxin {ECO:0000303|PubMed:19825616};
DE Short=OsCiTrx {ECO:0000303|PubMed:19825616};
DE Flags: Precursor;
GN ORFNames=OsI_29059 {ECO:0000312|EMBL:EAZ06817.1};
OS Oryza sativa subsp. indica (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=39946 {ECO:0000312|EMBL:EAZ06817.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [2]
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 play a role
CC in proper chloroplast development. {ECO:0000250|UniProtKB:Q9M7X9}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant CITRX-type
CC subfamily. {ECO:0000305}.
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DR EMBL; CM000133; EAZ06817.1; -; Genomic_DNA.
DR AlphaFoldDB; A2YUQ6; -.
DR SMR; A2YUQ6; -.
DR STRING; 39946.A2YUQ6; -.
DR PRIDE; A2YUQ6; -.
DR EnsemblPlants; BGIOSGA027053-TA; BGIOSGA027053-PA; BGIOSGA027053.
DR Gramene; BGIOSGA027053-TA; BGIOSGA027053-PA; BGIOSGA027053.
DR HOGENOM; CLU_110012_0_0_1; -.
DR OMA; PLQMMRD; -.
DR Proteomes; UP000007015; Chromosome 8.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:EnsemblPlants.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:EnsemblPlants.
DR GO; GO:0009657; P:plastid organization; IEA:EnsemblPlants.
DR InterPro; IPR044182; CITRX.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR47834; PTHR47834; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Chloroplast; Disulfide bond; Electron transport; Oxidoreductase; Plastid;
KW Redox-active center; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..189
FT /note="Thioredoxin-like protein CITRX, chloroplastic"
FT /id="PRO_0000430873"
FT DOMAIN 72..189
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 112
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT ACT_SITE 115
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 106
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 113
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 114
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT DISULFID 112..115
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 189 AA; 20512 MW; 39B0269CB10F3CE8 CRC64;
MAMAAAASLL PACAAPTLPG RAFRPRRNST PTASLSCDGG SRGRGVGLGV ILGGGRAQGV
RRNAAAETYV PGSGKYIAPD YLVKKVTAKE LEELVRGERK VPLIVDFYAT WCGPCVLMAQ
DIEMLAVEYE NNALFVKVDT DDEYELARDM QVRGLPTLYF FSPDQSKDAL RTEGLIPIDM
IRNIIDNEL
