TRXB_RICPR
ID TRXB_RICPR Reviewed; 310 AA.
AC Q9ZD97;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Thioredoxin reductase;
DE Short=TRXR;
DE EC=1.8.1.9;
GN Name=trxB; OrderedLocusNames=RP445;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P0A9P4};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P0A9P4};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A9P4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AJ235271; CAA14902.1; -; Genomic_DNA.
DR PIR; D71703; D71703.
DR RefSeq; NP_220826.1; NC_000963.1.
DR RefSeq; WP_004597668.1; NC_000963.1.
DR AlphaFoldDB; Q9ZD97; -.
DR SMR; Q9ZD97; -.
DR STRING; 272947.RP445; -.
DR EnsemblBacteria; CAA14902; CAA14902; CAA14902.
DR KEGG; rpr:RP445; -.
DR PATRIC; fig|272947.5.peg.458; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_1_5; -.
DR OMA; VDNFPGY; -.
DR Proteomes; UP000002480; Chromosome.
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 3: Inferred from homology;
KW Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..310
FT /note="Thioredoxin reductase"
FT /id="PRO_0000166743"
FT BINDING 34..41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT BINDING 281..290
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT DISULFID 135..138
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
SQ SEQUENCE 310 AA; 33582 MW; 573CA975C750957D CRC64;
MKITTKVLII GSGPAGLSAA IYTARSALKP ILINGMQPGG QLTMTTDVEN YPGFAETIQG
PWLMEQMSMQ AKNVGTEIIS DYVERVDLSK RPFKIFTGTG NEYEADSIII CTGAESKWLG
IASEQEFRGF GVSSCAICDG FFFKNQEIVV VGGGNSALEE ALYLTNHANK VTVVHRRNSF
RAEKILQDRL FKNPKISVIW DHIIDEIVGS NKPKAVTGVK IQNVYTNEIN LVNCSGVFIA
IGHAPNTALF KGQIAIDDDN YIVTQSGSTR TNVEGVFAAG DVQDKIYRQA VTAAASGCMA
ALEVAKFLNK