ID   THIO2_CORNE             Reviewed;         108 AA.
AC   P07887;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Thioredoxin C-2;
OS   Corynebacterium nephridii.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3040729; DOI=10.1016/s0021-9258(18)45323-9;
RA   Lim C.-J., Fuchs J.A., McFarlan S.C., Hogenkamp H.P.C.;
RT   "Cloning, expression, and nucleotide sequence of a gene encoding a second
RT   thioredoxin from Corynebacterium nephridii.";
RL   J. Biol. Chem. 262:12114-12119(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2917572; DOI=10.1111/j.1432-1033.1989.tb14565.x;
RA   McFarlan S.C., Hogenkamp H.P.C., Eccleston E.D., Howard J.B., Fuchs J.A.;
RT   "Purification, characterization and revised amino acid sequence of a second
RT   thioredoxin from Corynebacterium nephridii.";
RL   Eur. J. Biochem. 179:389-398(1989).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA23305.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X14630; CAA32779.1; -; Genomic_DNA.
DR   EMBL; J02801; AAA23305.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P07887; -.
DR   SMR; P07887; -.
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   CHAIN           2..108
FT                   /note="Thioredoxin C-2"
FT                   /id="PRO_0000120094"
FT   DOMAIN          2..108
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   108 AA;  11716 MW;  590A22FCDD093520 CRC64;
     MSATIVNTTD ENFQADVLDA ETPVLVDFWA GWCAPCKAIA PVLEELSNEY AGKVKIVKVD
     VTSCEDTAVK YNIRNIPALL MFKDGEVVAQ QVGAAPRSKL AAFIDQNI