TRXB_COXBU
ID TRXB_COXBU Reviewed; 320 AA.
AC P39916;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Thioredoxin reductase;
DE Short=TRXR;
DE EC=1.8.1.9;
GN Name=trxB; OrderedLocusNames=CBU_1193;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nine Mile phase I / Bratislava;
RA Oswald W.;
RL Thesis (1994), Justus Liebig University / Frankfurt, Germany.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; X75627; CAA53288.1; -; Genomic_DNA.
DR EMBL; AE016828; AAO90702.1; -; Genomic_DNA.
DR PIR; S43131; S43131.
DR RefSeq; NP_820188.1; NC_002971.3.
DR RefSeq; WP_005770716.1; NZ_CCYB01000035.1.
DR AlphaFoldDB; P39916; -.
DR SMR; P39916; -.
DR STRING; 227377.CBU_1193; -.
DR DNASU; 1209097; -.
DR EnsemblBacteria; AAO90702; AAO90702; CBU_1193.
DR GeneID; 1209097; -.
DR KEGG; cbu:CBU_1193; -.
DR PATRIC; fig|227377.7.peg.1190; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_1_6; -.
DR OMA; VDNFPGY; -.
DR Proteomes; UP000002671; 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 3: Inferred from homology;
KW Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..320
FT /note="Thioredoxin reductase"
FT /id="PRO_0000166728"
FT BINDING 36..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT BINDING 287..296
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT DISULFID 136..139
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT CONFLICT 21
FT /note="A -> D (in Ref. 1; CAA53288)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="A -> V (in Ref. 1; CAA53288)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="D -> A (in Ref. 1; CAA53288)"
FT /evidence="ECO:0000305"
FT CONFLICT 64..66
FT /note="QLM -> KLL (in Ref. 1; CAA53288)"
FT /evidence="ECO:0000305"
FT CONFLICT 74..77
FT /note="ERLD -> GGALN (in Ref. 1; CAA53288)"
FT /evidence="ECO:0000305"
FT CONFLICT 87..88
FT /note="EA -> KP (in Ref. 1; CAA53288)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="Q -> P (in Ref. 1; CAA53288)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="K -> Q (in Ref. 1; CAA53288)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="A -> P (in Ref. 1; CAA53288)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="G -> A (in Ref. 1; CAA53288)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="A -> S (in Ref. 1; CAA53288)"
FT /evidence="ECO:0000305"
FT CONFLICT 284..292
FT /note="AAGDVTDHV -> PAVVVRGQL (in Ref. 1; CAA53288)"
FT /evidence="ECO:0000305"
FT CONFLICT 296..298
FT /note="AIT -> TIA (in Ref. 1; CAA53288)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="A -> P (in Ref. 1; CAA53288)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 34620 MW; 750851B6FDDEB5E3 CRC64;
MNKPQHHSLI ILGSGPAGYT AAIYAARANL KPIMITGMEQ GGQLMTTTDV DNWPGEAPGL
QGPQLMERMQ KHAERLDTQF IFDHINEADL NQRPFLLKGD NATYSCDALI IATGASARYL
GLPSEKAYMG KGVSACATCD GFFYRGKKVA VVGGGNTAVE EALYLSHIAS HVTLIHRRDK
LRAEKMLSAQ LIKKVEEGKV AIVWSHVIEE VLGDDQGVTG VHLKHVKEEK TQDLTIDGLF
IAIGHDPNTK IFKEQLEMDE AGYLRAKSGL QGNATATNIP GVFAAGDVTD HVYRQAITAA
GMGCMAALDA ERYLDSLNQA
