ID   TRXB_PENCH              Reviewed;         334 AA.
AC   P43496;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   05-FEB-2025, entry version 106.
DE   RecName: Full=Thioredoxin reductase;
DE            EC=1.8.1.9;
GN   Name=TRR1; Synonyms=TRXB;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-29, FUNCTION, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 9480 / CBS 307.48 / NRRL 1951 / GB8 / QM 941;
RX   PubMed=8106340; DOI=10.1128/jb.176.4.973-984.1994;
RA   Cohen G., Argaman A., Schreiber R., Mislovati M., Aharonowitz Y.;
RT   "The thioredoxin system of Penicillium chrysogenum and its possible role in
RT   penicillin biosynthesis.";
RL   J. Bacteriol. 176:973-984(1994).
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       {ECO:0000269|PubMed:8106340}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC         NADPH + H(+); 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:0000269|PubMed:8106340}.
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; X76119; CAA53725.1; -; Genomic_DNA.
DR   PIR; B49888; B49888.
DR   AlphaFoldDB; P43496; -.
DR   SMR; P43496; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR050097; Ferredoxin-NADP_redctase_2.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   NCBIfam; TIGR01292; TRX_reduct; 1.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; NADP;
KW   Oxidoreductase; Redox-active center.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8106340"
FT   CHAIN           2..334
FT                   /note="Thioredoxin reductase"
FT                   /id="PRO_0000166765"
FT   BINDING         11..14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         40..41
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         45
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         54
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         148
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         294
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         301..303
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   DISULFID        145..148
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
SQ   SEQUENCE   334 AA;  35701 MW;  7A3A7457D7486341 CRC64;
     MVHSKVVIIG SGAGAHTAAI YLSRAELQPV LYEGMLANGT AAGGQLTTTT DVENFPGFPS
     GIGGAELMDN MRAQSERFGT EIITETISKL DLSSRPFKMW TEWNDDEGSE PVRTADAVII
     ATGANARRLN LPGEETYWQN GISACAVCDG AVPIFRNKPL YVIGGGDSAA EEAMFLAKYG
     SSVTVLVRKD KLRASNIMAD RLLAHPKCKV RFNTVATEVI GENKPNGLMT HLRVKDVLSN
     AEEVVEANGL FYAVGHDPAS GLVKGQVELD DEGYIITKPG TSFTNVEGVF ACGDVQDKRY
     RQAITSAGSG CVAALEAEKF IAETETHQEA KPVL
//