ID   TRXB_PNEJI              Reviewed;         327 AA.
AC   Q8J0U0;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Thioredoxin reductase;
DE            EC=1.8.1.9;
GN   Name=TRR1;
OS   Pneumocystis jirovecii (Human pneumocystis pneumonia agent).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis.
OX   NCBI_TaxID=42068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=12801645; DOI=10.1016/s0378-1119(03)00549-3;
RA   Kutty G.K., Huang S.N., Kovacs J.A.;
RT   "Characterization of thioredoxin reductase genes (trr1) from Pneumocystis
RT   carinii and Pneumocystis jiroveci.";
RL   Gene 310:175-183(2003).
CC   -!- FUNCTION: Component of the thioredoxin-thioredoxin reductase system
CC       which may be involved in biosynthesis of penicillins and cephalosporins
CC       and may be important in determining the thiol-disulfide redox balance.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC         H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P29509};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P29509};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P29509}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29509}.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AY130996; AAN12366.1; -; Genomic_DNA.
DR   EMBL; AF532986; AAP72145.1; -; mRNA.
DR   AlphaFoldDB; Q8J0U0; -.
DR   SMR; Q8J0U0; -.
DR   VEuPathDB; FungiDB:T551_03486; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN           1..327
FT                   /note="Thioredoxin reductase"
FT                   /id="PRO_0000166767"
FT   BINDING         10..13
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         39..40
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         44
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         53
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         86
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         143
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         286
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         293..295
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   DISULFID        140..143
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
SQ   SEQUENCE   327 AA;  35608 MW;  6A5D230F87BF5777 CRC64;
     MHSKVIIIGS GPAGHTAAIY LARAELKPVL YEGMLANGIA AGGQLTTTTD VENYPGFPDG
     IMGPLLMEKF REQSVKYGTC IITETVSKLD LSKRPFKYWC ESDENTCHTA DVVVMATGAY
     ARRLHIPGEE TYWQRGISAC AVCDGAAPIF RGKCLSVVGG GDSAAEESLF LTRYATKVYL
     LVRRDKLRAS AVMAKRLLNH PKIEVIWNTV VLRSLGDGHL LNRLEIKNVK TQVVSELHVS
     GLFYAIGHEP ATALVRGQVE CDDNGYIITK NGGPETNIKG FFAAGDVQDK KWRQAVTSAG
     SGCMAGLAAE RLLAEEEEMK NIEKNKK