ID   THIO_PENCH              Reviewed;         106 AA.
AC   P34723;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=TRXA;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-40.
RC   STRAIN=ATCC 9480 / CBS 307.48 / NRRL 1951 / GB8 / QM 941;
RX   PubMed=8106340; DOI=10.1128/jb.176.4.973-984.1994;
RA   Cohen G., Argaman A., Schreiber R., Mislovati M., Aharonowitz Y.;
RT   "The thioredoxin system of Penicillium chrysogenum and its possible role in
RT   penicillin biosynthesis.";
RL   J. Bacteriol. 176:973-984(1994).
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}.
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DR   EMBL; X76120; CAA53726.1; -; Genomic_DNA.
DR   PIR; A49888; A49888.
DR   AlphaFoldDB; P34723; -.
DR   SMR; P34723; -.
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   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   CHAIN           1..106
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120042"
FT   DOMAIN          2..106
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        32
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        35
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            26
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            33
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            34
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        32..35
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   106 AA;  11265 MW;  43FE12BFAA2DA786 CRC64;
     MGVTPIKSVA EYKEKVTDAT GPVVVDFHAT WCGPCKAIAP ALEKLSETHT GIQFYKVDVD
     ELSEVAASNG VSAMPTFHFY KGGERNEEVK GANPAAIQAG VKAILE