TRXB_STAAN
ID TRXB_STAAN Reviewed; 311 AA.
AC P99101; Q99VL2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Thioredoxin reductase;
DE Short=TRXR;
DE EC=1.8.1.9;
GN Name=trxB; OrderedLocusNames=SA0719;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=N315;
RX PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017;
RA Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y.,
RA Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C.,
RA Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.;
RT "Correlation of proteomic and transcriptomic profiles of Staphylococcus
RT aureus during the post-exponential phase of growth.";
RL J. Microbiol. Methods 60:247-257(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB41952.1; -; Genomic_DNA.
DR PIR; E89849; E89849.
DR RefSeq; WP_000134963.1; NC_002745.2.
DR AlphaFoldDB; P99101; -.
DR SMR; P99101; -.
DR SWISS-2DPAGE; P99101; -.
DR EnsemblBacteria; BAB41952; BAB41952; BAB41952.
DR KEGG; sau:SA0719; -.
DR HOGENOM; CLU_031864_5_1_9; -.
DR OMA; VDNFPGY; -.
DR Proteomes; UP000000751; 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 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Redox-active center.
FT CHAIN 1..311
FT /note="Thioredoxin reductase"
FT /id="PRO_0000166746"
FT BINDING 35..42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT BINDING 277..286
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT DISULFID 134..137
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
SQ SEQUENCE 311 AA; 33616 MW; 1A337DE3736C9265 CRC64;
MTEIDFDIAI IGAGPAGMTA AVYASRANLK TVMIERGIPG GQMANTEEVE NFPGFEMITG
PDLSTKMFEH AKKFGAVYQY GDIKSVEDKG EYKVINFGNK ELTAKAVIIA TGAEYKKIGV
PGEQELGGRG VSYCAVCDGA FFKNKRLFVI GGGDSAVEEG TFLTKFADKV TIVHRRDELR
AQRILQDRAF KNDKIDFIWS HTLKSINEKD GKVGSVTLTS TKDGSEETHE ADGVFIYIGM
KPLTAPFKDL GITNDVGYIV TKDDMTTSVP GIFAAGDVRD KGLRQIVTAT GDGSIAAQSA
AEYIEHLNDQ A