TRXB_STAAW
ID TRXB_STAAW Reviewed; 311 AA.
AC P66011; Q99VL2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Thioredoxin reductase;
DE Short=TRXR;
DE EC=1.8.1.9;
GN Name=trxB; OrderedLocusNames=MW0726;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB94591.1; -; Genomic_DNA.
DR RefSeq; WP_000134963.1; NC_003923.1.
DR PDB; 4GCM; X-ray; 1.80 A; A/B=1-311.
DR PDBsum; 4GCM; -.
DR AlphaFoldDB; P66011; -.
DR SMR; P66011; -.
DR EnsemblBacteria; BAB94591; BAB94591; BAB94591.
DR KEGG; sam:MW0726; -.
DR HOGENOM; CLU_031864_5_1_9; -.
DR OMA; VDNFPGY; -.
DR Proteomes; UP000000418; 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 3D-structure; Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP;
KW Oxidoreductase; Redox-active center.
FT CHAIN 1..311
FT /note="Thioredoxin reductase"
FT /id="PRO_0000166749"
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"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:4GCM"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:4GCM"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4GCM"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:4GCM"
FT TURN 121..126
FT /evidence="ECO:0007829|PDB:4GCM"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4GCM"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:4GCM"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:4GCM"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:4GCM"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:4GCM"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 200..209
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:4GCM"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:4GCM"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:4GCM"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4GCM"
FT HELIX 286..309
FT /evidence="ECO:0007829|PDB:4GCM"
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
