ID   THIO1_NOSSO             Reviewed;         107 AA.
AC   P0A4L2; P06544;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Thioredoxin 1;
DE            Short=Trx-1;
DE   AltName: Full=Thioredoxin-M;
GN   Name=trxA;
OS   Nostoc sp. (strain ATCC 29151 / PCC 7119) (Anabaena sp.).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=1168;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3096973; DOI=10.1128/jb.168.3.1258-1264.1986;
RA   Lim C.-J., Gleason F.K., Fuchs J.A.;
RT   "Cloning, expression, and characterization of the Anabaena thioredoxin gene
RT   in Escherichia coli.";
RL   J. Bacteriol. 168:1258-1264(1986).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-107.
RX   PubMed=3926769; DOI=10.1016/s0021-9258(17)39272-4;
RA   Gleason F.K., Whittaker M.M., Holmgren A., Joernvall H.;
RT   "The primary structure of thioredoxin from the filamentous cyanobacterium
RT   Anabaena sp. 7119.";
RL   J. Biol. Chem. 260:9567-9573(1985).
CC   -!- FUNCTION: Participates in various redox reactions through the
CC       reversible oxidation of its active center dithiol to a disulfide and
CC       catalyzes dithiol-disulfide exchange reactions.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; M14736; AAA22049.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0A4L2; -.
DR   SMR; P0A4L2; -.
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   PIRSF; PIRSF000077; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Electron transport;
KW   Redox-active center; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3926769"
FT   CHAIN           2..107
FT                   /note="Thioredoxin 1"
FT                   /id="PRO_0000120073"
FT   DOMAIN          2..107
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        32..35
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   107 AA;  11721 MW;  BC3841B6C2E240C9 CRC64;
     MSAAAQVTDS TFKQEVLDSD VPVLVDFWAP WCGPCRMVAP VVDEIAQQYE GKIKVVKVNT
     DENPQVASQY GIRSIPTLMI FKGGQKVDMV VGAVPKTTLS QTLEKHL