TRXB_PENCH
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 03-AUG-2022, entry version 97.
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 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: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 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 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