ID   THIO_ALIAC              Reviewed;         105 AA.
AC   P80579;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA;
OS   Alicyclobacillus acidocaldarius subsp. acidocaldarius (Bacillus
OS   acidocaldarius).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=1388;
RN   [1]
RP   PROTEIN SEQUENCE, CHARACTERIZATION, DISULFIDE BOND, AND MASS SPECTROMETRY.
RX   PubMed=9359865; DOI=10.1042/bj3280277;
RA   Bartolucci S., Guagliardi A., Pedone E., de Pascale D., Cannio R.,
RA   Camardella L., Rossi M., Nicastro G., de Chiara C., Facci P., Mascetti G.,
RA   Nicolini C.;
RT   "Thioredoxin from Bacillus acidocaldarius: characterization, high-level
RT   expression in Escherichia coli and molecular modelling.";
RL   Biochem. J. 328:277-285(1997).
RN   [2]
RP   STRUCTURE BY NMR.
RX   PubMed=10632710; DOI=10.1046/j.1432-1327.2000.01015.x;
RA   Nicastro G., De Chiara C., Pedone E., Tato M., Rossi M., Bartolucci S.;
RT   "NMR solution structure of a novel thioredoxin from bacillus acidocaldarius
RT   possible determinants of protein stability.";
RL   Eur. J. Biochem. 267:403-413(2000).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=12837806; DOI=10.1128/jb.185.14.4285-4289.2003;
RA   Bartolucci S., De Simone G., Galdiero S., Improta R., Menchise V.,
RA   Pedone C., Pedone E., Saviano M.;
RT   "An integrated structural and computational study of the thermostability of
RT   two thioredoxin mutants from Alicyclobacillus acidocaldarius.";
RL   J. Bacteriol. 185:4285-4289(2003).
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   -!- MASS SPECTROMETRY: Mass=11577; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9359865};
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   PDB; 1NSW; X-ray; 1.90 A; A/B/C/D=1-105.
DR   PDB; 1NW2; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-105.
DR   PDB; 1QUW; NMR; -; A=1-105.
DR   PDB; 1RQM; NMR; -; A=1-105.
DR   PDBsum; 1NSW; -.
DR   PDBsum; 1NW2; -.
DR   PDBsum; 1QUW; -.
DR   PDBsum; 1RQM; -.
DR   AlphaFoldDB; P80579; -.
DR   BMRB; P80579; -.
DR   SMR; P80579; -.
DR   EvolutionaryTrace; P80579; -.
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   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Electron transport; Redox-active center; Transport.
FT   CHAIN           1..105
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120072"
FT   DOMAIN          1..105
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        29..32
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT                   ECO:0000269|PubMed:9359865"
FT   STRAND          3..5
FT                   /evidence="ECO:0007829|PDB:1NW2"
FT   TURN            7..9
FT                   /evidence="ECO:0007829|PDB:1NSW"
FT   HELIX           10..14
FT                   /evidence="ECO:0007829|PDB:1NSW"
FT   STRAND          15..18
FT                   /evidence="ECO:0007829|PDB:1NSW"
FT   STRAND          20..25
FT                   /evidence="ECO:0007829|PDB:1NSW"
FT   HELIX           30..45
FT                   /evidence="ECO:0007829|PDB:1NSW"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:1NSW"
FT   STRAND          51..56
FT                   /evidence="ECO:0007829|PDB:1NSW"
FT   TURN            57..59
FT                   /evidence="ECO:0007829|PDB:1NSW"
FT   HELIX           61..66
FT                   /evidence="ECO:0007829|PDB:1NSW"
FT   STRAND          71..79
FT                   /evidence="ECO:0007829|PDB:1NSW"
FT   STRAND          82..89
FT                   /evidence="ECO:0007829|PDB:1NSW"
FT   HELIX           93..99
FT                   /evidence="ECO:0007829|PDB:1NSW"
FT   TURN            100..104
FT                   /evidence="ECO:0007829|PDB:1NSW"
SQ   SEQUENCE   105 AA;  11576 MW;  E03F636DFB3C3745 CRC64;
     ATMTLTDANF QQAIQGDKPV LVDFWAAWCG PCRMMAPVLE EFAEAHADKV TVAKLNVDEN
     PETTSQFGIM SIPTLILFKG GRPVKQLIGY QPKEQLEAQL ADVLQ