THIO1_CORNE
ID THIO1_CORNE Reviewed; 105 AA.
AC P00275;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Thioredoxin C-1;
OS Corynebacterium nephridii.
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=1722;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7021558; DOI=10.1016/s0021-9258(19)52524-8;
RA Meng M., Hogenkamp H.P.C.;
RT "Purification, characterization, and amino acid sequence of thioredoxin
RT from Corynebacterium nephridii.";
RL J. Biol. Chem. 256:9174-9182(1981).
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 PIR; A00281; TXFK.
DR AlphaFoldDB; P00275; -.
DR SMR; P00275; -.
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 CHAIN 1..105
FT /note="Thioredoxin C-1"
FT /id="PRO_0000120093"
FT DOMAIN 1..105
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 30..33
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 105 AA; 11279 MW; 028E8E31FE19FC31 CRC64;
ATVKVDNSNF QSDVLQSSEP VVVDFWAEWC GPCKMIAPAL DEIATEMAGQ VKIAKVNIDE
NPELAAQFGV RSIPTLLMFK DGELAANMVG AAPKSRLADW IKASA