ID   TRXB_PNECA              Reviewed;         325 AA.
AC   Q7Z7S3;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Thioredoxin reductase;
DE            EC=1.8.1.9;
GN   Name=TRR1;
OS   Pneumocystis carinii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis.
OX   NCBI_TaxID=4754;
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   -!- 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; AF532987; AAP72146.1; -; mRNA.
DR   EMBL; AF541944; AAP72148.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7Z7S3; -.
DR   SMR; Q7Z7S3; -.
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..325
FT                   /note="Thioredoxin reductase"
FT                   /id="PRO_0000166766"
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   325 AA;  35282 MW;  7363B063F8293730 CRC64;
     MHSKVVIIGS GPSGHTAAIY LGRAELKPIL YEGMLANGIA PGGQLTTTTD VENYPGFPDG
     ILGPSLMEAF RKQSEKYGAQ IITDTVSKLD LSKRPFKYCC ESNEEVFHTA DVVILATGAY
     ARRLNIPGEE IYWQRGISAC AVCDGAAPIF RGKPLAVVGG GDSAAEESLF LTRYATKVYL
     LVRRDKLRAS PIMAKRLLHH PKIEILWNTV ALESLGDNNL MNCVKIKNVK TQEVSELQVN
     GLFYAIGHEP ATTLVRGQVE CDKDGYIITK NGGPETNIKG FFAAGDVQDK KWRQAVTSAG
     SGCMAGLAAE RLLAEEEEMK NIEDS