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Database: UniProt
Entry: P0A9P4
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Original site: P0A9P4 
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   26-NOV-2014, entry version 89.
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:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC       Note=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   BindingDB; P0A9P4; -.
DR   DrugBank; DB03147; Flavin adenine dinucleotide.
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   InParanoid; P0A9P4; -.
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-KW.
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: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       {ECO:0000244|PDB:1TRB}.
FT   HELIX        16     26       {ECO:0000244|PDB:1TRB}.
FT   TURN         27     29       {ECO:0000244|PDB:1TRB}.
FT   STRAND       33     35       {ECO:0000244|PDB:1TRB}.
FT   HELIX        42     46       {ECO:0000244|PDB:1TRB}.
FT   HELIX        62     75       {ECO:0000244|PDB:1TRB}.
FT   STRAND       79     81       {ECO:0000244|PDB:1TRB}.
FT   STRAND       85     89       {ECO:0000244|PDB:1TRB}.
FT   STRAND       91    101       {ECO:0000244|PDB:1TRB}.
FT   STRAND      103    111       {ECO:0000244|PDB:1TRB}.
FT   STRAND      115    117       {ECO:0000244|PDB:1TRB}.
FT   HELIX       123    127       {ECO:0000244|PDB:1TRB}.
FT   TURN        130    132       {ECO:0000244|PDB:1TRB}.
FT   STRAND      133    135       {ECO:0000244|PDB:1TRB}.
FT   HELIX       137    140       {ECO:0000244|PDB:1TRB}.
FT   HELIX       141    144       {ECO:0000244|PDB:1TRB}.
FT   STRAND      147    152       {ECO:0000244|PDB:1TRB}.
FT   HELIX       156    165       {ECO:0000244|PDB:1TRB}.
FT   TURN        166    168       {ECO:0000244|PDB:1TRB}.
FT   STRAND      169    175       {ECO:0000244|PDB:1TRB}.
FT   STRAND      177    180       {ECO:0000244|PDB:1TRB}.
FT   HELIX       185    196       {ECO:0000244|PDB:1TRB}.
FT   STRAND      198    203       {ECO:0000244|PDB:1TRB}.
FT   STRAND      207    213       {ECO:0000244|PDB:1TRB}.
FT   STRAND      215    224       {ECO:0000244|PDB:1TRB}.
FT   STRAND      227    229       {ECO:0000244|PDB:1CL0}.
FT   STRAND      233    236       {ECO:0000244|PDB:1TRB}.
FT   STRAND      238    242       {ECO:0000244|PDB:1TRB}.
FT   STRAND      246    249       {ECO:0000244|PDB:1TRB}.
FT   HELIX       251    253       {ECO:0000244|PDB:1TRB}.
FT   TURN        254    256       {ECO:0000244|PDB:1TRB}.
FT   STRAND      269    272       {ECO:0000244|PDB:1TRB}.
FT   STRAND      282    284       {ECO:0000244|PDB:1TRB}.
FT   HELIX       286    289       {ECO:0000244|PDB:1TRB}.
FT   STRAND      291    293       {ECO:0000244|PDB:1TRB}.
FT   HELIX       296    314       {ECO:0000244|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
//
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