ID   THIO2_SYNY3             Reviewed;         109 AA.
AC   P73263;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 135.
DE   RecName: Full=Thioredoxin-like protein slr1139;
GN   OrderedLocusNames=slr1139;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-19.
RX   PubMed=9298645; DOI=10.1002/elps.1150180806;
RA   Sazuka T., Ohara O.;
RT   "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT   PCC6803: linking 130 protein spots with their respective genes.";
RL   Electrophoresis 18:1252-1258(1997).
CC   -!- INTERACTION:
CC       P73263; P73728: sll1621; NbExp=4; IntAct=EBI-862065, EBI-862771;
CC       P73263; P73348: slr1198; NbExp=2; IntAct=EBI-862065, EBI-862753;
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA17291.1; -; Genomic_DNA.
DR   PIR; S77444; S77444.
DR   AlphaFoldDB; P73263; -.
DR   SMR; P73263; -.
DR   IntAct; P73263; 19.
DR   STRING; 1148.1652369; -.
DR   PaxDb; P73263; -.
DR   EnsemblBacteria; BAA17291; BAA17291; BAA17291.
DR   KEGG; syn:slr1139; -.
DR   eggNOG; COG3118; Bacteria.
DR   InParanoid; P73263; -.
DR   OMA; HEGAITK; -.
DR   PhylomeDB; P73263; -.
DR   BRENDA; 1.11.1.24; 6192.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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   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; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9298645"
FT   CHAIN           2..109
FT                   /note="Thioredoxin-like protein slr1139"
FT                   /id="PRO_0000120140"
FT   DOMAIN          2..107
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        31..34
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   109 AA;  12171 MW;  C2AFC18F72A35BBC CRC64;
     MSLLEITDAE FEQETQGQTK PVLVYFWASW CGPCRLMAPA IQAIAKDYGD KLKVLKLEVD
     PNPAAVAQCK VEGVPALRLF KNNELVMTHE GAIAKPKLLE LLKEELDFI