ID   THIO1_SYNE7             Reviewed;         107 AA.
AC   P12243; Q79N44;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Thioredoxin 1;
DE            Short=Trx-1;
DE   AltName: Full=Thioredoxin-M {ECO:0000303|PubMed:2492995};
GN   Name=trxA; Synonyms=trxM {ECO:0000303|PubMed:2492995};
GN   OrderedLocusNames=Synpcc7942_1830;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2492995; DOI=10.1016/s0021-9258(19)84953-0;
RA   Muller E.G.D., Buchanan B.B.;
RT   "Thioredoxin is essential for photosynthetic growth. The thioredoxin m gene
RT   of Anacystis nidulans.";
RL   J. Biol. Chem. 264:4008-4014(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Holtman C.K., Sandoval P., Chen Y., Socias T., McMurtry S., Gonzalez A.,
RA   Salinas I., Golden S.S., Youderian P.;
RT   "Synechococcus elongatus PCC7942 cosmid 4G8.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; J04475; AAA22057.1; -; Genomic_DNA.
DR   EMBL; AY157498; AAN46173.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57860.1; -; Genomic_DNA.
DR   RefSeq; WP_011244574.1; NC_007604.1.
DR   AlphaFoldDB; P12243; -.
DR   SMR; P12243; -.
DR   STRING; 1140.Synpcc7942_1830; -.
DR   PRIDE; P12243; -.
DR   EnsemblBacteria; ABB57860; ABB57860; Synpcc7942_1830.
DR   KEGG; syf:Synpcc7942_1830; -.
DR   eggNOG; COG3118; Bacteria.
DR   HOGENOM; CLU_090389_10_2_3; -.
DR   OMA; QVGVAPK; -.
DR   OrthoDB; 1630944at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1830-MON; -.
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   3: Inferred from homology;
KW   Disulfide bond; Electron transport; Redox-active center; Transport.
FT   CHAIN           1..107
FT                   /note="Thioredoxin 1"
FT                   /id="PRO_0000120137"
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;  11648 MW;  B81D6D19C9168607 CRC64;
     MSVAAAVTDA TFKQEVLESS IPVLVDFWAP WCGPCRMVAP VVDEIAQQYS DQVKVVKVNT
     DENPSVASQY GIRSIPTLMI FKDGQRVDTV VGAVPKTTLA NTLDKHL