ID   TYPX_TRYBB              Reviewed;         144 AA.
AC   O77404;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Tryparedoxin;
DE            Short=TryX;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9714547; DOI=10.1016/s0014-5793(98)00793-5;
RA   Luedemann H., Dormeyer M., Sticherling C., Stallmann D., Follmann H.,
RA   Krauth-Siegel R.L.;
RT   "Trypanosoma brucei tryparedoxin, a thioredoxin-like protein in African
RT   trypanosomes.";
RL   FEBS Lett. 431:381-385(1998).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS).
RX   PubMed=12707277; DOI=10.1074/jbc.m301526200;
RA   Alphey M.S., Gabrielsen M., Micossi E., Leonard G.A., McSweeney S.M.,
RA   Ravelli R.B., Tetaud E., Fairlamb A.H., Bond C.S., Hunter W.N.;
RT   "Tryparedoxins from Crithidia fasciculata and Trypanosoma brucei:
RT   photoreduction of the redox disulfide using synchrotron radiation and
RT   evidence for a conformational switch implicated in function.";
RL   J. Biol. Chem. 278:25919-25925(2003).
CC   -!- FUNCTION: Acts as a thiol-disulfide oxidoreductase. It is spontaneously
CC       reduced by trypanothione.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ006403; CAA07003.1; -; mRNA.
DR   PDB; 1O73; X-ray; 2.28 A; A=1-144.
DR   PDB; 6GXG; X-ray; 1.60 A; A=2-142, B/C=2-144.
DR   PDB; 6GXY; X-ray; 1.80 A; A/B/C=2-144.
DR   PDBsum; 1O73; -.
DR   PDBsum; 6GXG; -.
DR   PDBsum; 6GXY; -.
DR   AlphaFoldDB; O77404; -.
DR   SASBDB; O77404; -.
DR   SMR; O77404; -.
DR   EvolutionaryTrace; O77404; -.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:InterPro.
DR   CDD; cd03009; TryX_like_TryX_NRX; 1.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR045870; TryX_NRX_thioredoxin_dom.
DR   Pfam; PF13905; Thioredoxin_8; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Electron transport; Redox-active center;
KW   Transport.
FT   CHAIN           1..144
FT                   /note="Tryparedoxin"
FT                   /id="PRO_0000120066"
FT   DOMAIN          2..144
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        40..43
FT                   /note="Redox-active"
FT   TURN            3..7
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   STRAND          13..15
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   STRAND          17..19
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   HELIX           23..26
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   STRAND          30..36
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   HELIX           41..57
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   TURN            58..62
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   STRAND          63..69
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   HELIX           74..81
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   STRAND          85..88
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   HELIX           91..96
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   HELIX           97..104
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   STRAND          108..116
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   TURN            117..119
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   STRAND          122..125
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   HELIX           127..133
FT                   /evidence="ECO:0007829|PDB:6GXG"
FT   STRAND          136..139
FT                   /evidence="ECO:0007829|PDB:6GXG"
SQ   SEQUENCE   144 AA;  15891 MW;  3FF6725F668462E1 CRC64;
     MSGLAKYLPG ATNLLSKSGE VSLGSLVGKT VFLYFSASWC PPCRGFTPVL AEFYEKHHVA
     KNFEVVLISW DENESDFHDY YGKMPWLALP FDQRSTVSEL GKTFGVESIP TLITINADTG
     AIIGTQARTR VIEDPDGANF PWPN