ID   THIO_STRCL              Reviewed;         107 AA.
AC   Q05739;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   24-JAN-2024, entry version 100.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA;
OS   Streptomyces clavuligerus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
RX   PubMed=8349555; DOI=10.1128/jb.175.16.5159-5167.1993;
RA   Cohen G., Yanko M., Mislovati M., Argaman A., Schreiber R., Av-Gay Y.,
RA   Aharonowitz Y.;
RT   "Thioredoxin-thioredoxin reductase system of Streptomyces clavuligerus:
RT   sequences, expression, and organization of the genes.";
RL   J. Bacteriol. 175:5159-5167(1993).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
RX   PubMed=8423136; DOI=10.1128/jb.175.3.623-629.1993;
RA   Aharonowitz Y., Av-Gay Y., Schreiber R., Cohen G.;
RT   "Characterization of a broad-range disulfide reductase from Streptomyces
RT   clavuligerus and its possible role in beta-lactam antibiotic
RT   biosynthesis.";
RL   J. Bacteriol. 175:623-629(1993).
CC   -!- FUNCTION: Component of the thioredoxin-thioredoxin reductase system.
CC       Participates in various redox reactions through the reversible
CC       oxidation of its active center dithiol to a disulfide and catalyzes
CC       dithiol-disulfide exchange reactions.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z21946; CAA79941.1; -; Genomic_DNA.
DR   PIR; B53307; B53307.
DR   AlphaFoldDB; Q05739; -.
DR   SMR; Q05739; -.
DR   STRING; 1901.BB341_14070; -.
DR   eggNOG; COG3118; Bacteria.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01068; thioredoxin; 1.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; Thioredoxin; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Electron transport; Redox-active center; Transport.
FT   CHAIN           1..107
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120135"
FT   DOMAIN          2..107
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        33..36
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   107 AA;  11483 MW;  9AB62438E065EFAF CRC64;
     MAGVLKNVTD DTFEADVLKS EKPVLVDFWA EWCGPCRQIA PSLEAITEHG GQIEIVKLNI
     DQNPATAAKY GVMSIPTLNV YQGGEVVKTI VGAKPKAALL RPGPVPR
//