TRXB_HELPY
ID TRXB_HELPY Reviewed; 311 AA.
AC P56431;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Thioredoxin reductase;
DE Short=TRXR;
DE EC=1.8.1.9;
GN Name=trxB; OrderedLocusNames=HP_0825;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD07875.1; -; Genomic_DNA.
DR PIR; A64623; A64623.
DR RefSeq; NP_207618.1; NC_000915.1.
DR RefSeq; WP_000564420.1; NC_018939.1.
DR PDB; 2Q0K; X-ray; 1.70 A; A/B=1-311.
DR PDB; 2Q0L; X-ray; 1.45 A; A/B=1-311.
DR PDB; 3ISH; X-ray; 2.43 A; A/B/C=1-311.
DR PDBsum; 2Q0K; -.
DR PDBsum; 2Q0L; -.
DR PDBsum; 3ISH; -.
DR AlphaFoldDB; P56431; -.
DR SMR; P56431; -.
DR DIP; DIP-3417N; -.
DR IntAct; P56431; 8.
DR MINT; P56431; -.
DR STRING; 85962.C694_04225; -.
DR PaxDb; P56431; -.
DR EnsemblBacteria; AAD07875; AAD07875; HP_0825.
DR KEGG; hpy:HP_0825; -.
DR PATRIC; fig|85962.47.peg.879; -.
DR eggNOG; COG0492; Bacteria.
DR OMA; VDNFPGY; -.
DR PhylomeDB; P56431; -.
DR EvolutionaryTrace; P56431; -.
DR Proteomes; UP000000429; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP;
KW Oxidoreductase; Redox-active center; Reference proteome.
FT CHAIN 1..311
FT /note="Thioredoxin reductase"
FT /id="PRO_0000166733"
FT BINDING 31..39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 32..39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT BINDING 281..290
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT DISULFID 133..136
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2Q0L"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:2Q0L"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:2Q0L"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2Q0L"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:2Q0L"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:2Q0L"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:2Q0L"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:2Q0L"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2Q0L"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:2Q0L"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2Q0L"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2Q0L"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:2Q0L"
FT HELIX 290..309
FT /evidence="ECO:0007829|PDB:2Q0L"
SQ SEQUENCE 311 AA; 33538 MW; 0718EFE4A43A478D CRC64;
MIDCAIIGGG PAGLSAGLYA TRGGVKNAVL FEKGMPGGQI TGSSEIENYP GVKEVVSGLD
FMQPWQEQCF RFGLKHEMTA VQRVSKKDSH FVILAEDGKT FEAKSVIIAT GGSPKRTGIK
GESEYWGKGV STCATCDGFF YKNKEVAVLG GGDTAVEEAI YLANICKKVY LIHRRDGFRC
APITLEHAKN NDKIEFLTPY VVEEIKGDAS GVSSLSIKNT ATNEKRELVV PGFFIFVGYD
VNNAVLKQED NSMLCKCDEY GSIVVDFSMK TNVQGLFAAG DIRIFAPKQV VCAASDGATA
ALSVISYLEH H
