ID Q81FS4_BACCR Unreviewed; 326 AA.
AC Q81FS4;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:AAP08475.1};
DE EC=1.8.1.9 {ECO:0000313|EMBL:AAP08475.1};
GN OrderedLocusNames=BC_1495 {ECO:0000313|EMBL:AAP08475.1};
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP08475.1, ECO:0000313|Proteomes:UP000001417};
RN [1] {ECO:0000313|EMBL:AAP08475.1, ECO:0000313|Proteomes:UP000001417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC 9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
RN [2] {ECO:0007829|PDB:7A76}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH FAD.
RX PubMed=33326741; DOI=10.1021/acs.biochem.0c00745;
RA Hammerstad M., Gudim I., Hersleth H.P.;
RT "The Crystal Structures of Bacillithiol Disulfide Reductase Bdr (YpdA)
RT Provide Structural and Functional Insight into a New Type of FAD-Containing
RT NADPH-Dependent Oxidoreductase.";
RL Biochemistry 59:4793-4798(2020).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; AE016877; AAP08475.1; -; Genomic_DNA.
DR RefSeq; NP_831274.1; NC_004722.1.
DR RefSeq; WP_001168520.1; NC_004722.1.
DR PDB; 7A76; X-ray; 1.65 A; A/B/C/D=1-326.
DR AlphaFoldDB; Q81FS4; -.
DR SMR; Q81FS4; -.
DR KEGG; bce:BC1495; -.
DR PATRIC; fig|226900.8.peg.1472; -.
DR HOGENOM; CLU_067342_0_0_9; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR023856; Bdr.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR NCBIfam; TIGR04018; Bthiol_YpdA; 1.
DR PANTHER; PTHR48105:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF13738; Pyr_redox_3; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7A76}; FAD {ECO:0007829|PDB:7A76};
KW Flavoprotein {ECO:0007829|PDB:7A76};
KW Nucleotide-binding {ECO:0007829|PDB:7A76};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AAP08475.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001417}.
FT BINDING 14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:7A76"
FT BINDING 33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:7A76"
FT BINDING 34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:7A76"
FT BINDING 39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:7A76"
FT BINDING 44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:7A76"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:7A76"
FT BINDING 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:7A76"
FT BINDING 97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:7A76"
FT BINDING 295
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:7A76"
FT BINDING 307
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:7A76"
FT BINDING 308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:7A76"
SQ SEQUENCE 326 AA; 36479 MW; F26673D845557F7C CRC64;
MQKETVIIIG GGPCGLAAAI SLQKVGINPL VIEKGNIVNA IYNYPTHQTF FSSSEKLEIG
DVAFITENRK PVRNQALAYY REVVRRKSVR VNAFERVEKV QKDGEAFQVE TTKRDGSKEI
YIAKYIVVAT GYYDNPNYMN VPGEELKKVA HYFKEGHPYF DRDVVVIGGK NSSVDAALEL
VKSGARVTVL YRGIEYSPSI KPWILPEFEA LVRNGTIQMH FGAHVKEITE HTLTFTVDGE
ALTIKNDFVF AMTGYHPDHS FLTKMGVQID EETGRPFYTE DRMETNAENI FIAGVIAAGN
NANEIFIENG RFHGDAIAQT IASREK
//
