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Entry: P0A9P4
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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-OCT-2014, entry version 87.
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 277:1453-1462(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
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; 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
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. {ECO:0000269|PubMed:10947986}.
CC   -!- INTERACTION:
CC       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; 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   DIP; DIP-6168N; -.
DR   IntAct; P0A9P4; 15.
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; HINEVDF; -.
DR   OrthoDB; EOG65XN2W; -.
DR   PhylomeDB; P0A9P4; -.
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   PRO; PR: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:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:CACAO.
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. {ECO:0000269|PubMed:1575737}.
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                                {ECO:0000269|PubMed:8114095}.
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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