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Thioredoxin 1 (Trx-1)

 THIO_ECOLI              Reviewed;         109 AA.
P0AA25; P00274; P76750; Q2M889; Q47674; Q8XAT2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 126.
RecName: Full=Thioredoxin 1;
Short=Trx-1;
Name=trxA; Synonyms=fipA, tsnC; OrderedLocusNames=b3781, JW5856;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6098320; DOI=10.1007/BF01116889;
Hoeoeg J.-O., von Bahr-Lindstroem H., Josephson S., Wallace B.J.,
Kushner S.R., Joernvall H., Holmgren A.;
"Nucleotide sequence of the thioredoxin gene from Escherichia coli.";
Biosci. Rep. 4:917-923(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6099324; DOI=10.1016/0378-1119(84)90015-5;
Wallace B.J., Kushner S.R.;
"Genetic and physical analysis of the thioredoxin (trxA) gene of
Escherichia coli K-12.";
Gene 32:399-408(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3891733;
Lim C.-J., Geraghty D., Fuchs J.A.;
"Cloning and nucleotide sequence of the trxA gene of Escherichia coli
K-12.";
J. Bacteriol. 163:311-316(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Wallace B.J., Zownir O., Kushner S.R.;
"Physical analysis of the thioredoxin gene from Escherichia coli K-
12.";
(In) Holmgren A. (eds.);
Thioredoxin and glutaredoxin systems, structure and function,
pp.11-19, Raven Press, New York (1986).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=1379743; DOI=10.1126/science.1379743;
Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
"Analysis of the Escherichia coli genome: DNA sequence of the region
from 84.5 to 86.5 minutes.";
Science 257:771-778(1992).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[8]
PROTEIN SEQUENCE OF 2-109.
STRAIN=B;
PubMed=4883076; DOI=10.1111/j.1432-1033.1968.tb00470.x;
Holmgren A.;
"Thioredoxin. 6. The amino acid sequence of the protein from
Escherichia coli B.";
Eur. J. Biochem. 6:475-484(1968).
[9]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[11]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=1094461; DOI=10.1073/pnas.72.6.2305;
Holmgren A., Soederberg B.-O., Eklund H., Braenden C.-I.;
"Three-dimensional structure of Escherichia coli thioredoxin-S2 to
2.8-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 72:2305-2309(1975).
[12]
X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS).
PubMed=4616096; DOI=10.1016/0022-2836(74)90262-9;
Soederberg B.-O., Holmgren A., Braenden C.-I.;
"Structure of oxidized thioredoxin to 4 with 5-A resolution.";
J. Mol. Biol. 90:143-152(1974).
[13]
X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS).
PubMed=2181145; DOI=10.1016/0022-2836(90)90313-B;
Katti S.K., le Master D.M., Eklund H.;
"Crystal structure of thioredoxin from Escherichia coli at 1.68-A
resolution.";
J. Mol. Biol. 212:167-184(1990).
[14]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT GLU-37.
PubMed=8098620; DOI=10.1021/bi00070a017;
Nikkola M., Gleason F.K., Fuchs J.A., Eklund H.;
"Crystal structure analysis of a mutant Escherichia coli thioredoxin
in which lysine 36 is replaced by glutamic acid.";
Biochemistry 32:5093-5098(1993).
[15]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND DISULFIDE BOND.
PubMed=10489448; DOI=10.1107/S0907444999008756;
Schultz L.W., Chivers P.T., Raines R.T.;
"The CXXC motif: crystal structure of an active-site variant of
Escherichia coli thioredoxin.";
Acta Crystallogr. D 55:1533-1538(1999).
[16]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TRXB.
PubMed=10947986; DOI=10.1126/science.289.5482.1190;
Lennon B.W., Williams C.H. Jr., Ludwig M.L.;
"Twists in catalysis: alternating conformations of Escherichia coli
thioredoxin reductase.";
Science 289:1190-1194(2000).
[17]
STRUCTURE BY NMR.
PubMed=2193685; DOI=10.1021/bi00469a016;
Dyson H.J., Gippert G.P., Case D.A., Holmgren A., Wright P.E.;
"Three-dimensional solution structure of the reduced form of
Escherichia coli thioredoxin determined by nuclear magnetic resonance
spectroscopy.";
Biochemistry 29:4129-4136(1990).
[18]
STRUCTURE BY NMR.
PubMed=7812718; DOI=10.1016/S0969-2126(94)00086-7;
Jeng M.F., Campbell A.P., Begley T., Holmgren A., Case D.A.,
Wright P.E., Dyson H.J.;
"High-resolution solution structures of oxidized and reduced
Escherichia coli thioredoxin.";
Structure 2:853-868(1994).
-!- FUNCTION: Participates in various redox reactions through the
reversible oxidation of its active center dithiol to a disulfide
and catalyzes dithiol-disulfide exchange reactions.
-!- SUBUNIT: Monomer. Interacts with bacteriophage T3 DNA polymerase.
{ECO:0000269|PubMed:10947986}.
-!- INTERACTION:
P00581:5 (xeno); NbExp=3; IntAct=EBI-368542, EBI-8664634;
O22160:At2g44920 (xeno); NbExp=2; IntAct=EBI-368542, EBI-2895776;
Q9SCY2:FKBP13 (xeno); NbExp=2; IntAct=EBI-368542, EBI-2895757;
Q9LXX5:PPD6 (xeno); NbExp=2; IntAct=EBI-368542, EBI-2895738;
Q9LU86:PRXQ (xeno); NbExp=2; IntAct=EBI-368542, EBI-540311;
P23321:PSBO1 (xeno); NbExp=2; IntAct=EBI-368542, EBI-449414;
Q9S841:PSBO2 (xeno); NbExp=2; IntAct=EBI-368542, EBI-449424;
P81760:TL17 (xeno); NbExp=2; IntAct=EBI-368542, EBI-449573;
P82281:TL29 (xeno); NbExp=2; IntAct=EBI-368542, EBI-2895799;
P0A9P4:trxB; NbExp=2; IntAct=EBI-368542, EBI-1029826;
Q39249:VDE1 (xeno); NbExp=2; IntAct=EBI-368542, EBI-2895666;
-!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA24534.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAA67582.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; M26133; AAA24693.1; -; Genomic_DNA.
EMBL; K02845; AAA24534.1; ALT_INIT; Genomic_DNA.
EMBL; M10424; AAA24533.1; -; Genomic_DNA.
EMBL; M54881; AAA24696.1; -; Genomic_DNA.
EMBL; M12779; AAA24694.1; -; Genomic_DNA.
EMBL; M87049; AAA67582.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC76786.2; -; Genomic_DNA.
EMBL; AP009048; BAE77517.1; -; Genomic_DNA.
PIR; A91519; TXEC.
RefSeq; NP_418228.2; NC_000913.3.
RefSeq; WP_001280776.1; NZ_LN832404.1.
PDB; 1F6M; X-ray; 2.95 A; C/D/G/H=2-109.
PDB; 1KEB; X-ray; 1.80 A; A/B=2-109.
PDB; 1M7T; NMR; -; A=32-108.
PDB; 1OAZ; X-ray; 2.78 A; A/B=2-109.
PDB; 1SKR; X-ray; 2.40 A; B=2-109.
PDB; 1SKS; X-ray; 2.30 A; B=2-109.
PDB; 1SKW; X-ray; 2.30 A; B=2-109.
PDB; 1SL0; X-ray; 3.20 A; B/D=2-109.
PDB; 1SL1; X-ray; 2.20 A; B=2-109.
PDB; 1SL2; X-ray; 2.30 A; B=2-109.
PDB; 1SRX; X-ray; 2.80 A; A=2-109.
PDB; 1T7P; X-ray; 2.20 A; B=2-109.
PDB; 1T8E; X-ray; 2.54 A; B=2-109.
PDB; 1THO; X-ray; 2.30 A; A=2-109.
PDB; 1TK0; X-ray; 2.30 A; B=2-109.
PDB; 1TK5; X-ray; 2.20 A; B=2-109.
PDB; 1TK8; X-ray; 2.50 A; B=2-109.
PDB; 1TKD; X-ray; 2.49 A; B=2-109.
PDB; 1TXX; X-ray; 2.20 A; A=2-109.
PDB; 1X9M; X-ray; 2.10 A; B=2-109.
PDB; 1X9S; X-ray; 2.70 A; B=2-109.
PDB; 1X9W; X-ray; 2.30 A; B=2-109.
PDB; 1XOA; NMR; -; A=2-109.
PDB; 1XOB; NMR; -; A=2-109.
PDB; 1ZCP; X-ray; 2.30 A; A/B/C/D=2-109.
PDB; 1ZYQ; X-ray; 2.70 A; B=2-109.
PDB; 1ZZY; X-ray; 2.50 A; A/B=2-109.
PDB; 2AJQ; X-ray; 2.60 A; B/I=2-109.
PDB; 2BTO; X-ray; 2.50 A; T=2-109.
PDB; 2EIO; X-ray; 2.60 A; A/B/C/D=2-109.
PDB; 2EIQ; X-ray; 1.90 A; A/B=2-109.
PDB; 2EIR; X-ray; 2.50 A; A/B/C/D=2-109.
PDB; 2FCH; X-ray; 2.60 A; A/B/C/D/E/F/G=2-109.
PDB; 2FD3; X-ray; 2.45 A; A/B=2-109.
PDB; 2H6X; X-ray; 2.60 A; A/B=2-109.
PDB; 2H6Y; X-ray; 2.40 A; A/B=2-109.
PDB; 2H6Z; X-ray; 2.25 A; A/B=2-109.
PDB; 2H70; X-ray; 2.70 A; A/B=2-109.
PDB; 2H71; X-ray; 2.20 A; A/B=2-109.
PDB; 2H72; X-ray; 2.25 A; A/B=2-109.
PDB; 2H73; X-ray; 2.45 A; A/B=2-109.
PDB; 2H74; X-ray; 2.40 A; A/B=4-109.
PDB; 2H75; X-ray; 2.20 A; A/B=2-109.
PDB; 2H76; X-ray; 2.25 A; A/B=2-109.
PDB; 2O8V; X-ray; 3.00 A; B=2-109.
PDB; 2TIR; X-ray; 2.00 A; A=2-109.
PDB; 2TRX; X-ray; 1.68 A; A/B=2-109.
PDB; 3DYR; X-ray; 2.00 A; A/B=2-109.
PDB; 4HU7; X-ray; 1.40 A; A/B=2-109.
PDB; 4HU9; X-ray; 1.55 A; A=2-109.
PDB; 4HUA; X-ray; 1.10 A; A=2-109.
PDB; 4X43; X-ray; 1.65 A; A/B/C=2-109.
PDB; 5HR0; X-ray; 1.31 A; A/B=1-109.
PDB; 5HR1; X-ray; 2.14 A; A/B/C/D/E/F/G=1-107.
PDB; 5HR2; X-ray; 1.20 A; A=1-109.
PDB; 5HR3; X-ray; 1.10 A; A/B=1-109.
PDBsum; 1F6M; -.
PDBsum; 1KEB; -.
PDBsum; 1M7T; -.
PDBsum; 1OAZ; -.
PDBsum; 1SKR; -.
PDBsum; 1SKS; -.
PDBsum; 1SKW; -.
PDBsum; 1SL0; -.
PDBsum; 1SL1; -.
PDBsum; 1SL2; -.
PDBsum; 1SRX; -.
PDBsum; 1T7P; -.
PDBsum; 1T8E; -.
PDBsum; 1THO; -.
PDBsum; 1TK0; -.
PDBsum; 1TK5; -.
PDBsum; 1TK8; -.
PDBsum; 1TKD; -.
PDBsum; 1TXX; -.
PDBsum; 1X9M; -.
PDBsum; 1X9S; -.
PDBsum; 1X9W; -.
PDBsum; 1XOA; -.
PDBsum; 1XOB; -.
PDBsum; 1ZCP; -.
PDBsum; 1ZYQ; -.
PDBsum; 1ZZY; -.
PDBsum; 2AJQ; -.
PDBsum; 2BTO; -.
PDBsum; 2EIO; -.
PDBsum; 2EIQ; -.
PDBsum; 2EIR; -.
PDBsum; 2FCH; -.
PDBsum; 2FD3; -.
PDBsum; 2H6X; -.
PDBsum; 2H6Y; -.
PDBsum; 2H6Z; -.
PDBsum; 2H70; -.
PDBsum; 2H71; -.
PDBsum; 2H72; -.
PDBsum; 2H73; -.
PDBsum; 2H74; -.
PDBsum; 2H75; -.
PDBsum; 2H76; -.
PDBsum; 2O8V; -.
PDBsum; 2TIR; -.
PDBsum; 2TRX; -.
PDBsum; 3DYR; -.
PDBsum; 4HU7; -.
PDBsum; 4HU9; -.
PDBsum; 4HUA; -.
PDBsum; 4X43; -.
PDBsum; 5HR0; -.
PDBsum; 5HR1; -.
PDBsum; 5HR2; -.
PDBsum; 5HR3; -.
ProteinModelPortal; P0AA25; -.
SMR; P0AA25; -.
BioGrid; 4263316; 300.
DIP; DIP-31856N; -.
IntAct; P0AA25; 99.
MINT; P0AA25; -.
STRING; 316385.ECDH10B_3970; -.
CarbonylDB; P0AA25; -.
iPTMnet; P0AA25; -.
SWISS-2DPAGE; P0AA25; -.
EPD; P0AA25; -.
PaxDb; P0AA25; -.
PRIDE; P0AA25; -.
EnsemblBacteria; AAC76786; AAC76786; b3781.
EnsemblBacteria; BAE77517; BAE77517; BAE77517.
GeneID; 31656514; -.
GeneID; 948289; -.
KEGG; ecj:JW5856; -.
KEGG; eco:b3781; -.
PATRIC; fig|511145.12.peg.3896; -.
EchoBASE; EB1024; -.
EcoGene; EG11031; trxA.
eggNOG; COG0526; LUCA.
HOGENOM; HOG000292977; -.
InParanoid; P0AA25; -.
KO; K03671; -.
OMA; DANQEFA; -.
PhylomeDB; P0AA25; -.
BioCyc; EcoCyc:RED-THIOREDOXIN-MONOMER; -.
BioCyc; MetaCyc:RED-THIOREDOXIN-MONOMER; -.
EvolutionaryTrace; P0AA25; -.
PRO; PR:P0AA25; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IBA:GO_Central.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IDA:EcoCyc.
GO; GO:0047134; F:protein-disulfide reductase activity; IBA:GO_Central.
GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
GO; GO:0045454; P:cell redox homeostasis; IMP:EcoCyc.
GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR005746; Thioredoxin.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
PANTHER; PTHR10438; PTHR10438; 1.
Pfam; PF00085; Thioredoxin; 1.
PIRSF; PIRSF000077; Thioredoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR01068; thioredoxin; 1.
PROSITE; PS00194; THIOREDOXIN_1; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Disulfide bond; Electron transport;
Host-virus interaction; Redox-active center; Reference proteome;
Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:4883076}.
CHAIN 2 109 Thioredoxin 1.
/FTId=PRO_0000120096.
DOMAIN 2 109 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 33 33 Nucleophile.
ACT_SITE 36 36 Nucleophile.
SITE 27 27 Deprotonates C-terminal active site Cys.
SITE 34 34 Contributes to redox potential value.
SITE 35 35 Contributes to redox potential value.
MOD_RES 70 70 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
DISULFID 33 36 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691,
ECO:0000269|PubMed:10489448}.
CONFLICT 72 73 GI -> IG (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 88 88 A -> AS (in Ref. 5; AAA24696).
{ECO:0000305}.
STRAND 5 8 {ECO:0000244|PDB:4HUA}.
TURN 10 12 {ECO:0000244|PDB:4HUA}.
HELIX 13 16 {ECO:0000244|PDB:4HUA}.
TURN 17 19 {ECO:0000244|PDB:4HUA}.
STRAND 22 29 {ECO:0000244|PDB:4HUA}.
HELIX 34 49 {ECO:0000244|PDB:4HUA}.
TURN 50 53 {ECO:0000244|PDB:4HUA}.
STRAND 55 60 {ECO:0000244|PDB:4HUA}.
TURN 61 63 {ECO:0000244|PDB:4HUA}.
HELIX 65 70 {ECO:0000244|PDB:4HUA}.
STRAND 75 83 {ECO:0000244|PDB:4HUA}.
STRAND 86 93 {ECO:0000244|PDB:4HUA}.
HELIX 97 105 {ECO:0000244|PDB:4HUA}.
SEQUENCE 109 AA; 11807 MW; EF5933EA29668EE9 CRC64;
MSDKIIHLTD DSFDTDVLKA DGAILVDFWA EWCGPCKMIA PILDEIADEY QGKLTVAKLN
IDQNPGTAPK YGIRGIPTLL LFKNGEVAAT KVGALSKGQL KEFLDANLA


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U1123p CLIA Peroxiredoxin-2,Pig,PRDX2,Sus scrofa,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E1123p ELISA Peroxiredoxin-2,Pig,PRDX2,Sus scrofa,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E2222r HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2
E1123p ELISA kit Peroxiredoxin-2,Pig,PRDX2,Sus scrofa,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T


 

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