TRXB_ECOLI
ID TRXB_ECOLI Reviewed; 321 AA.
AC P0A9P4; P09625;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Thioredoxin reductase;
DE Short=TRXR;
DE EC=1.8.1.9;
GN Name=trxB; OrderedLocusNames=b0888, JW0871;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3288628; DOI=10.1016/s0021-9258(18)68409-1;
RA Russel M., Model P.;
RT "Sequence of thioredoxin reductase from Escherichia coli. Relationship to
RT other flavoprotein disulfide oxidoreductases.";
RL J. Biol. Chem. 263:9015-9019(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-321.
RC STRAIN=K12;
RX PubMed=8380150; DOI=10.1128/jb.175.1.166-175.1993;
RA Delaney J.M., Wall D., Georgopoulos C.;
RT "Molecular characterization of the Escherichia coli htrD gene: cloning,
RT sequence, regulation, and involvement with cytochrome d oxidase.";
RL J. Bacteriol. 175:166-175(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-321.
RX PubMed=7934832; DOI=10.1111/j.1365-2958.1993.tb02673.x;
RA Poole R.K., Hatch L., Cleeter M.W.J., Gibson F., Cox G.B., Wu G.;
RT "Cytochrome bd biosynthesis in Escherichia coli: the sequences of the cydC
RT and cydD genes suggest that they encode the components of an ABC membrane
RT transporter.";
RL Mol. Microbiol. 10:421-430(1993).
RN [7]
RP PROTEIN SEQUENCE OF 2-26.
RX PubMed=1575737; DOI=10.1016/0006-291x(92)90636-y;
RA Ueshima R., Fujita N., Ishihama A.;
RT "Identification of Escherichia coli proteins cross-reacting with antibodies
RT against region 2.2 peptide of RNA polymerase sigma subunit.";
RL Biochem. Biophys. Res. Commun. 184:634-639(1992).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=2067578; DOI=10.1038/352172a0;
RA Kuriyan J., Krishna T.S.R., Wong L., Guenther B., Pahler A.,
RA Williams C.H. Jr., Model P.;
RT "Convergent evolution of similar function in two structurally divergent
RT enzymes.";
RL Nature 352:172-174(1991).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BOND, FAD BINDING SITES,
RP AND COFACTOR.
RX PubMed=8114095; DOI=10.1006/jmbi.1994.1190;
RA Waksman G., Krishna T.S.R., Williams C.H. Jr., Kuriyan J.;
RT "Crystal structure of Escherichia coli thioredoxin reductase refined at 2-A
RT resolution. Implications for a large conformational change during
RT catalysis.";
RL J. Mol. Biol. 236:800-816(1994).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=10595539; DOI=10.1110/ps.8.11.2366;
RA Lennon B.W., Williams C.H. Jr., Ludwig M.L.;
RT "Crystal structure of reduced thioredoxin reductase from Escherichia coli:
RT structural flexibility in the isoalloxazine ring of the flavin adenine
RT dinucleotide cofactor.";
RL Protein Sci. 8:2366-2379(1999).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TRXA, AND SUBUNIT.
RX PubMed=10947986; DOI=10.1126/science.289.5482.1190;
RA Lennon B.W., Williams C.H. Jr., Ludwig M.L.;
RT "Twists in catalysis: alternating conformations of Escherichia coli
RT thioredoxin reductase.";
RL Science 289:1190-1194(2000).
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:0000269|PubMed:8114095};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:8114095};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10947986}.
CC -!- INTERACTION:
CC P0A9P4; P0AA25: trxA; NbExp=2; IntAct=EBI-1029826, EBI-368542;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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; J03762; AAA24697.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73974.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35613.1; -; Genomic_DNA.
DR EMBL; L21749; AAA66170.1; -; Genomic_DNA.
DR EMBL; M95935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A28074; RDECT.
DR RefSeq; NP_415408.1; NC_000913.3.
DR RefSeq; WP_000537418.1; NZ_STEB01000006.1.
DR PDB; 1CL0; X-ray; 2.50 A; A=2-321.
DR PDB; 1F6M; X-ray; 2.95 A; A/B/E/F=2-321.
DR PDB; 1TDE; X-ray; 2.10 A; A=2-317.
DR PDB; 1TDF; X-ray; 2.30 A; A=2-317.
DR PDB; 1TRB; X-ray; 2.00 A; A=2-321.
DR PDBsum; 1CL0; -.
DR PDBsum; 1F6M; -.
DR PDBsum; 1TDE; -.
DR PDBsum; 1TDF; -.
DR PDBsum; 1TRB; -.
DR AlphaFoldDB; P0A9P4; -.
DR SMR; P0A9P4; -.
DR BioGRID; 4261715; 76.
DR BioGRID; 853298; 11.
DR ComplexPortal; CPX-2149; Thioredoxin reductase complex.
DR DIP; DIP-6168N; -.
DR IntAct; P0A9P4; 15.
DR STRING; 511145.b0888; -.
DR BindingDB; P0A9P4; -.
DR ChEMBL; CHEMBL3638339; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR SWISS-2DPAGE; P0A9P4; -.
DR jPOST; P0A9P4; -.
DR PaxDb; P0A9P4; -.
DR PRIDE; P0A9P4; -.
DR EnsemblBacteria; AAC73974; AAC73974; b0888.
DR EnsemblBacteria; BAA35613; BAA35613; BAA35613.
DR GeneID; 66670838; -.
DR GeneID; 949054; -.
DR KEGG; ecj:JW0871; -.
DR KEGG; eco:b0888; -.
DR PATRIC; fig|1411691.4.peg.1390; -.
DR EchoBASE; EB1025; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_1_6; -.
DR InParanoid; P0A9P4; -.
DR OMA; VDNFPGY; -.
DR PhylomeDB; P0A9P4; -.
DR BioCyc; EcoCyc:THIOREDOXIN-REDUCT-NADPH-MON; -.
DR BioCyc; MetaCyc:THIOREDOXIN-REDUCT-NADPH-MON; -.
DR BRENDA; 1.8.1.9; 2026.
DR SABIO-RK; P0A9P4; -.
DR EvolutionaryTrace; P0A9P4; -.
DR PRO; PR:P0A9P4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1902515; C:thioredoxin-disulfide reductase complex; IPI:ComplexPortal.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:CACAO.
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; Direct protein sequencing; Disulfide bond; FAD;
KW Flavoprotein; NADP; Oxidoreductase; Redox-active center;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1575737"
FT CHAIN 2..321
FT /note="Thioredoxin reductase"
FT /id="PRO_0000166729"
FT BINDING 36..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8114095"
FT BINDING 287..296
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8114095"
FT DISULFID 136..139
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:8114095"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:1TRB"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:1TRB"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1TRB"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:1TRB"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1TRB"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:1TRB"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1TRB"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:1TRB"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1TRB"
FT HELIX 156..165
FT /evidence="ECO:0007829|PDB:1TRB"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:1TRB"
FT HELIX 185..196
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 215..224
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1CL0"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:1TRB"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1TRB"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:1TRB"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:1TRB"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1TRB"
FT HELIX 296..314
FT /evidence="ECO:0007829|PDB:1TRB"
SQ SEQUENCE 321 AA; 34623 MW; 8E5AF86FB195CC82 CRC64;
MGTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV ENWPGDPNDL
TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD NGEYTCDALI IATGASARYL
GLPSEEAFKG RGVSACATCD GFFYRNQKVA VIGGGNTAVE EALYLSNIAS EVHLIHRRDG
FRAEKILIKR LMDKVENGNI ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL
FVAIGHSPNT AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA
GTGCMAALDA ERYLDGLADA K
