TRXB_STRCO
ID TRXB_STRCO Reviewed; 322 AA.
AC P52215;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Thioredoxin reductase;
DE Short=TRXR;
DE EC=1.8.1.9 {ECO:0000250|UniProtKB:P9WHH1};
GN Name=trxB {ECO:0000303|PubMed:9795152}; OrderedLocusNames=SCO3890;
GN ORFNames=SCH24.12c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=9795152; DOI=10.1016/s0378-1119(98)00357-6;
RA Gal-Mor O., Borovok I., Av-Gay Y., Cohen G., Aharonowitz Y.;
RT "Gene organization in the trxA/B-oriC region of the Streptomyces coelicolor
RT chromosome and comparison with other eubacteria.";
RL Gene 217:83-90(1998).
RN [2]
RP SEQUENCE REVISION.
RA Aharonowitz Y.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [4]
RP INDUCTION.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=9755177; DOI=10.1093/emboj/17.19.5776;
RA Paget M.S., Kang J.G., Roe J.H., Buttner M.J.;
RT "sigmaR, an RNA polymerase sigma factor that modulates expression of the
RT thioredoxin system in response to oxidative stress in Streptomyces
RT coelicolor A3(2).";
RL EMBO J. 17:5776-5782(1998).
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 Evidence={ECO:0000250|UniProtKB:P9WHH1};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P9WHH1};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P9WHH1};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WHH1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Expressed from 2 promoters, 1 of which (trxBp1) is under
CC control of SigR, and further transiently induced (about 50-fold) by the
CC thiol-oxidizing agent diamide. Part of the trxB-trxA operon.
CC {ECO:0000269|PubMed:9755177}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000250|UniProtKB:P9WHH1}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; X92105; CAA63076.1; -; Genomic_DNA.
DR EMBL; X92104; CAA63075.1; -; Genomic_DNA.
DR EMBL; AJ007313; CAA07451.1; -; Genomic_DNA.
DR EMBL; AL939118; CAB42713.1; -; Genomic_DNA.
DR PIR; T36577; T36577.
DR PIR; T42062; T42062.
DR RefSeq; NP_628076.1; NC_003888.3.
DR AlphaFoldDB; P52215; -.
DR SMR; P52215; -.
DR STRING; 100226.SCO3890; -.
DR GeneID; 1099326; -.
DR KEGG; sco:SCO3890; -.
DR PATRIC; fig|100226.15.peg.3963; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_1_11; -.
DR InParanoid; P52215; -.
DR PhylomeDB; P52215; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..322
FT /note="Thioredoxin reductase"
FT /id="PRO_0000166753"
FT BINDING 12..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 34..42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 176
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 239
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 259
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 286..289
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 286
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT DISULFID 136..139
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT CONFLICT 26
FT /note="A -> R (in Ref. 1; CAA63075/CAA07451)"
FT /evidence="ECO:0000305"
FT CONFLICT 73..74
FT /note="ER -> DG (in Ref. 1; CAA63075/CAA07451)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="Missing (in Ref. 1; CAA63075)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="G -> A (in Ref. 1; CAA63075)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="Missing (in Ref. 1; CAA63075)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="V -> L (in Ref. 3; CAB42713)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="P -> R (in Ref. 3; CAB42713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 34156 MW; 1B337B1742E3C457 CRC64;
MSDVRNVIII GSGPAGYTAA LYTARASLKP LVFEGAVTAG GALMNTTEVE NFPGFQDGIM
GPELMDNMRA QAERFGAELI PDDVVAVDLS GEIKTVTDTA GTVHRAKAVI VTTGSQHRKL
GLPNEDALSG RGVSWCATCD GFFFKDQDIA VIGGGDTAME EATFLSRFAK SVTIVHRRDT
LRASKAMQER AFADPKISFV WDSEVAEVQG DQKLAGLKLR NVKTGELSDL PVTGLFIAIG
HDPRTELFKG QLDLDPEGYL KVDAPSTRTN LTGVFGAGDV VDHTYRQAIT AAGTGCSAAV
DAEPFLAALS DEDKAEPEKT AV
