ID   TRXF_PEA                Reviewed;         182 AA.
AC   P29450;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Thioredoxin F-type, chloroplastic;
DE            Short=Trx-F;
DE   Flags: Precursor;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=1581563; DOI=10.1007/bf00019224;
RA   Lepiniec L., Hodges M., Gadal P., Cretin C.;
RT   "Isolation, characterization and nucleotide sequence of a full-length pea
RT   cDNA encoding thioredoxin-f.";
RL   Plant Mol. Biol. 18:1023-1025(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8642611; DOI=10.1007/bf02498636;
RA   Sahrawy M., Hecht V., Lopez Jaramillo J., Chueca A., Chartier Y., Meyer Y.;
RT   "Intron position as an evolutionary marker of thioredoxins and thioredoxin
RT   domains.";
RL   J. Mol. Evol. 42:422-431(1996).
CC   -!- FUNCTION: Participates in various redox reactions through the
CC       reversible oxidation of the active center dithiol to a disulfide. The F
CC       form is known to activate a number of enzymes of the photosynthetic
CC       carbon cycle.
CC   -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
CC       reductase (FTR) and ferredoxin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. Plant F-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X63537; CAA45098.1; -; mRNA.
DR   EMBL; U35830; AAC49357.1; -; Genomic_DNA.
DR   PIR; S20929; S20929.
DR   AlphaFoldDB; P29450; -.
DR   SMR; P29450; -.
DR   EnsemblPlants; Psat3g102640.1; Psat3g102640.1.cds; Psat3g102640.
DR   Gramene; Psat3g102640.1; Psat3g102640.1.cds; Psat3g102640.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Disulfide bond; Electron transport; Plastid;
KW   Redox-active center; Transit peptide; Transport.
FT   TRANSIT         1..69
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           70..182
FT                   /note="Thioredoxin F-type, chloroplastic"
FT                   /id="PRO_0000034160"
FT   DOMAIN          70..181
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        106
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        109
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            100
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            107
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            108
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        106..109
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   182 AA;  19775 MW;  158FC352CB9E0FF1 CRC64;
     MALNLCTSPK WIGTTVFDSA SSSKPSLASS FSTTSFSSSI LCSKRVGLQR LSLRRSISVS
     VRSSLETAGP TVTVGKVTEV NKDTFWPIVN AAGDKTVVLD MFTKWCGPCK VIAPLYEELS
     QKYLDVVFLK LDCNQDNKSL AKELGIKVVP TFKILKDNKI VKEVTGAKFD DLVAAIDTVR
     SS