ID   TRXF_MESCR              Reviewed;         191 AA.
AC   O81332;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Thioredoxin F-type, chloroplastic;
DE            Short=Trx-F;
DE   Flags: Precursor;
OS   Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Aizoaceae; Mesembryanthemum;
OC   Mesembryanthemum subgen. Cryophytum.
OX   NCBI_TaxID=3544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Michalowski C.B., Bohnert H.J.;
RT   "A cDNA for Thioredoxin F precursor from the common ice plant.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
CC       reductase (FTR) and ferredoxin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. Plant F-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF069314; AAC19392.1; -; mRNA.
DR   PIR; T12261; T12261.
DR   AlphaFoldDB; O81332; -.
DR   SMR; O81332; -.
DR   PRIDE; O81332; -.
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..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..191
FT                   /note="Thioredoxin F-type, chloroplastic"
FT                   /id="PRO_0000034159"
FT   DOMAIN          68..190
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        115
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        118
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            109
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            116
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            117
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        115..118
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   191 AA;  20641 MW;  D4FB462C4AE1980D CRC64;
     MAMQLSLSHQ SWAKSLASPI TSFDPARSPP KRVELGPNCL NGGATAGKLM REKVGERMRM
     SGRSCCVKAS LETAVGAESE TLVGKVTEVD KDTFWPIANG AGDKPVVLDM YTQWCGPCKV
     MAPKYQELAE KLLDVVFLKL DCNQENKPLA KELGIRVVPT FKILKGGKIV DEVTGAKFDK
     LVAAIEAARS S