ID   THIO_CERSP              Reviewed;         106 AA.
AC   P08058;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Y;
RX   PubMed=2137818; DOI=10.1128/jb.172.3.1556-1561.1990;
RA   Pille S., Chuat J.-C., Breton A.M., Clement-Metral J.D., Galibert F.;
RT   "Cloning, nucleotide sequence, and expression of the Rhodobacter
RT   sphaeroides Y thioredoxin gene.";
RL   J. Bacteriol. 172:1556-1561(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-106.
RC   STRAIN=Y;
RX   PubMed=3280308; DOI=10.1111/j.1432-1033.1988.tb13902.x;
RA   Clement-Metral J.D., Holmgren A., Cambillau C., Joernvall H., Eklund H.,
RA   Thomas D., Lederer F.;
RT   "Amino acid sequence determination and three-dimensional modelling of
RT   thioredoxin from the photosynthetic bacterium Rhodobacter sphaeroides Y.";
RL   Eur. J. Biochem. 172:413-419(1988).
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; M33806; AAA26182.1; -; Genomic_DNA.
DR   PIR; A35135; A35135.
DR   RefSeq; WP_002722246.1; NZ_WTFI01000013.1.
DR   AlphaFoldDB; P08058; -.
DR   SMR; P08058; -.
DR   GeneID; 57468874; -.
DR   GeneID; 67448292; -.
DR   OMA; QVGVAPK; -.
DR   OrthoDB; 1630944at2; -.
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                   /evidence="ECO:0000269|PubMed:3280308"
FT   CHAIN           2..106
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120122"
FT   DOMAIN          2..106
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        31..34
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   CONFLICT        61
FT                   /note="E -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   106 AA;  11343 MW;  9AD0AA94EE3BEFA4 CRC64;
     MSTVPVTDAT FDTEVRKSDV PVVVDFWAEW CGPCRQIGPA LEELSKEYAG KVKIVKVNVD
     ENPESPAMLG VRGIPALFLF KNGQVVSNKV GAAPKAALAT WIASAL