ID   THIO3_CORNE             Reviewed;         145 AA.
AC   P52228;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Thioredoxin C-3;
OS   Corynebacterium nephridii.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8652661; DOI=10.1016/0167-4781(96)00038-3;
RA   Lim C.-J., Sa J., Fuchs J.A.;
RT   "Identification of a third thioredoxin gene from Corynebacterium
RT   nephridii.";
RL   Biochim. Biophys. Acta 1307:13-16(1996).
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; U43655; AAB06490.1; -; Genomic_DNA.
DR   AlphaFoldDB; P52228; -.
DR   SMR; P52228; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   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; Heme; Iron; Metal-binding;
KW   Redox-active center; Transport.
FT   CHAIN           1..145
FT                   /note="Thioredoxin C-3"
FT                   /id="PRO_0000120095"
FT   DOMAIN          29..140
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   BINDING         25
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT   BINDING         28
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT   BINDING         29
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   DISULFID        65..68
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   145 AA;  16198 MW;  A3FB1A16CAB1BAD0 CRC64;
     MIIVCASCGA KNRVPEEKLA VHPNCGQCHQ ALLPLEPIEL NEQNFSNFIS NSDLPVLIDL
     WAEWCGPCKM MAPHFAQVAK QNPYVVFAKI DTEANPRLSA AFNVRSIPTL VLMNKTTEVA
     RISGALRTLE LQQWLDQQLQ QQQGN