(data stored in SCRATCH3701 zone)

SWISSPROT: TRXB_RICTY

ID   TRXB_RICTY              Reviewed;         310 AA.
AC   Q68WT3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 90.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB; OrderedLocusNames=RT0432;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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}.
DR   EMBL; AE017197; AAU03909.1; -; Genomic_DNA.
DR   RefSeq; WP_011190893.1; NC_006142.1.
DR   SMR; Q68WT3; -.
DR   STRING; 257363.RT0432; -.
DR   EnsemblBacteria; AAU03909; AAU03909; RT0432.
DR   KEGG; rty:RT0432; -.
DR   eggNOG; ENOG4105C3M; Bacteria.
DR   eggNOG; COG0492; LUCA.
DR   HOGENOM; HOG000072912; -.
DR   KO; K00384; -.
DR   OMA; VDNFPGY; -.
DR   OrthoDB; 692968at2; -.
DR   BioCyc; RTYP257363:G1G0L-439-MONOMER; -.
DR   Proteomes; UP000000604; 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;
DR   PRODOM; Q68WT3.
DR   SWISS-2DPAGE; Q68WT3.
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN           1..310
FT                   /note="Thioredoxin reductase"
FT                   /id="PRO_0000274792"
FT   NP_BIND         34..41
FT                   /note="FAD"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   NP_BIND         281..290
FT                   /note="FAD"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   DISULFID        135..138
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
SQ   SEQUENCE   310 AA;  33699 MW;  C1D1EB4A96A5DE49 CRC64;
     MKITTKVLII GSGPAGLSAA IYTARSSLKP ILINGMQPGG QLTMTTDVEN YPGFAKTIQG
     PWLMEQMSIQ AKNVGTEIIN DYVERVDLSK RPFKIFTGTG NKYEADSIII CTGAESKWLG
     ITSEQEFRGF GVSSCAICDG FFFKNQDIVV VGGGNSALEE ALYLTNHANK VTVVHRRNSF
     RAEKILQDRL FKNPKISVIW DHVIDEIVGS NQPKTVTGVK IKNVYTNEIN LVNCSGVFIA
     IGHTPNTTLF NGQIAIDDDN YIITQTGSTR TSVEGVFAAG DVQDKIYRQA ITAAASGCMA
     ALEVAKFLNK
//

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