TRXB_STRCL
ID TRXB_STRCL Reviewed; 322 AA.
AC Q05741;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Thioredoxin reductase {ECO:0000303|PubMed:8349555};
DE Short=TRXR;
DE EC=1.8.1.9 {ECO:0000269|PubMed:8349555};
GN Name=trxB {ECO:0000303|PubMed:8349555};
OS Streptomyces clavuligerus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1901;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-33, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC 3585 / VKM Ac-602;
RX PubMed=8349555; DOI=10.1128/jb.175.16.5159-5167.1993;
RA Cohen G., Yanko M., Mislovati M., Argaman A., Schreiber R., Av-Gay Y.,
RA Aharonowitz Y.;
RT "Thioredoxin-thioredoxin reductase system of Streptomyces clavuligerus:
RT sequences, expression, and organization of the genes.";
RL J. Bacteriol. 175:5159-5167(1993).
RN [2]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC 3585 / VKM Ac-602;
RX PubMed=8423136; DOI=10.1128/jb.175.3.623-629.1993;
RA Aharonowitz Y., Av-Gay Y., Schreiber R., Cohen G.;
RT "Characterization of a broad-range disulfide reductase from Streptomyces
RT clavuligerus and its possible role in beta-lactam antibiotic
RT biosynthesis.";
RL J. Bacteriol. 175:623-629(1993).
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:8423136}.
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:0000269|PubMed:8349555};
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:0000269|PubMed:8423136}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z21946; CAA79940.1; -; Genomic_DNA.
DR PIR; A53307; A53307.
DR RefSeq; WP_003956511.1; NZ_CP032052.1.
DR AlphaFoldDB; Q05741; -.
DR SMR; Q05741; -.
DR STRING; 443255.SCLAV_2898; -.
DR GeneID; 61470992; -.
DR eggNOG; COG0492; Bacteria.
DR OMA; VDNFPGY; -.
DR OrthoDB; 692968at2; -.
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:8349555"
FT CHAIN 2..322
FT /note="Thioredoxin reductase"
FT /id="PRO_0000166752"
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 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"
SQ SEQUENCE 322 AA; 34146 MW; 6D9AE0EBF43A8E26 CRC64;
MSDVRNVIII GSGPAGYTAA LYTARASLQP LVFEGAVTAG GALMNTTDVE NFPGFRDGIM
GPDLMDNMRA QAERFGAELI PDDVVSVDLT GDIKTVTDSA GTVHRAKAVI VTTGSQHRKL
GLPREDALSG RGVSWCATCD GFFFKDQDIV VVGGGDTAME EATFLSRFAK SVTIVHRRDS
LRASKAMQDR AFADPKISFA WNSEVATIHG EQKLTGLTLR DTKTGETREL AATGLFIAVG
HDPRTELFKG QLDLDDEGYL KVASPSTRTN LTGVFAAGDV VDHTYRQAIT AAGTGCSAAL
DAERYLAALA DSEQIAEPAP AV
