THIO_THIRO
ID THIO_THIRO Reviewed; 91 AA.
AC P96132;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
DE Flags: Fragment;
GN Name=trxA;
OS Thiocapsa roseopersicina.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=1058;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M1;
RA Haverkamp T., Schwenn J.D.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; U75512; AAB36882.1; -; Genomic_DNA.
DR AlphaFoldDB; P96132; -.
DR SMR; P96132; -.
DR STRING; 1058.SAMN05421783_110106; -.
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 3: Inferred from homology;
KW Disulfide bond; Electron transport; Redox-active center; Transport.
FT CHAIN 1..>91
FT /note="Thioredoxin"
FT /id="PRO_0000120141"
FT DOMAIN 2..>91
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"
FT NON_TER 91
SQ SEQUENCE 91 AA; 10209 MW; 385DC641F42585D4 CRC64;
MSDSIVHVTD DSFEDEVLKS LEPVLVDYWA DWCGPCKMIA PVLDEIAGEY AGRIKVAKLN
IDENPNTPRR YGIRGIPTLM LSRQSEVEAT K