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 01-MAY-2013, entry version 78.
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; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3288628;
RA Russel M., Model P.;
RT "Sequence of thioredoxin reductase from Escherichia coli. Relationship
RT to 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.,
RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA Yano M., Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT corresponding to 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.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(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
RT MG1655 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;
RA Delaney J.M., Wall D., Georgopoulos C.;
RT "Molecular characterization of the Escherichia coli htrD gene:
RT cloning, sequence, regulation, and involvement with cytochrome d
RT oxidase.";
RL J. Bacteriol. 175:166-175(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-321.
RX PubMed=7934832;
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
RT cydC and cydD genes suggest that they encode the components of an ABC
RT membrane 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
RT antibodies against region 2.2 peptide of RNA polymerase sigma
RT 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.,
RA 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
RT divergent enzymes.";
RL Nature 352:172-174(1991).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND DISULFIDE BOND.
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
RT at 2-A resolution. Implications for a large conformational change
RT during catalysis.";
RL J. Mol. Biol. 236:800-816(1994).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=10595539;
RA Lennon B.W., Williams C.H. Jr., Ludwig M.L.;
RT "Crystal structure of reduced thioredoxin reductase from Escherichia
RT coli: structural flexibility in the isoalloxazine ring of the flavin
RT adenine dinucleotide cofactor.";
RL Protein Sci. 8:2366-2379(1999).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TRXA.
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: Thioredoxin + NADP(+) = thioredoxin disulfide
CC + NADPH.
CC -!- COFACTOR: Binds 1 FAD per subunit.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P18843:nadE; NbExp=1; IntAct=EBI-1029826, EBI-548960;
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.
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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_000913.2.
DR RefSeq; YP_489160.1; NC_007779.1.
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 ProteinModelPortal; P0A9P4; -.
DR SMR; P0A9P4; 2-316.
DR IntAct; P0A9P4; 5.
DR STRING; 511145.b0888; -.
DR SWISS-2DPAGE; P0A9P4; -.
DR PaxDb; P0A9P4; -.
DR PRIDE; P0A9P4; -.
DR EnsemblBacteria; AAC73974; AAC73974; b0888.
DR EnsemblBacteria; BAA35613; BAA35613; BAA35613.
DR GeneID; 12932721; -.
DR GeneID; 949054; -.
DR KEGG; ecj:Y75_p0860; -.
DR KEGG; eco:b0888; -.
DR PATRIC; 32116985; VBIEscCol129921_0917.
DR EchoBASE; EB1025; -.
DR EcoGene; EG11032; trxB.
DR eggNOG; COG0492; -.
DR HOGENOM; HOG000072912; -.
DR KO; K00384; -.
DR OMA; VMGAFIA; -.
DR ProtClustDB; PRK10262; -.
DR BioCyc; EcoCyc:THIOREDOXIN-REDUCT-NADPH-MONOMER; -.
DR BioCyc; ECOL316407:JW0871-MONOMER; -.
DR BioCyc; MetaCyc:THIOREDOXIN-REDUCT-NADPH-MONOMER; -.
DR SABIO-RK; P0A9P4; -.
DR EvolutionaryTrace; P0A9P4; -.
DR Genevestigator; P0A9P4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:EcoCyc.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
DR InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom.
DR InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
DR InterPro; IPR005982; Thioredox_Rdtase.
DR Pfam; PF00070; Pyr_redox; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Redox-active center; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 321 Thioredoxin reductase.
FT /FTId=PRO_0000166729.
FT NP_BIND 36 43 FAD.
FT NP_BIND 287 296 FAD.
FT DISULFID 136 139 Redox-active.
FT STRAND 4 12
FT HELIX 16 26
FT TURN 27 29
FT STRAND 33 35
FT HELIX 42 46
FT HELIX 62 75
FT STRAND 79 81
FT STRAND 85 89
FT STRAND 91 101
FT STRAND 103 111
FT STRAND 115 117
FT HELIX 123 127
FT TURN 130 132
FT STRAND 133 135
FT HELIX 137 140
FT HELIX 141 144
FT STRAND 147 152
FT HELIX 156 165
FT TURN 166 168
FT STRAND 169 175
FT STRAND 177 180
FT HELIX 185 196
FT STRAND 198 203
FT STRAND 207 213
FT STRAND 215 224
FT STRAND 227 229
FT STRAND 233 236
FT STRAND 238 242
FT STRAND 246 249
FT HELIX 251 253
FT TURN 254 256
FT STRAND 269 272
FT STRAND 282 284
FT HELIX 286 289
FT STRAND 291 293
FT HELIX 296 314
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
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