THIO2_ECOLI
ID THIO2_ECOLI Reviewed; 139 AA.
AC P0AGG4; P33636; P76593; P77000; P77001;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Thioredoxin 2;
DE Short=Trx-2;
DE EC=1.8.1.8;
DE AltName: Full=Protein-disulfide reductase;
GN Name=trxC; Synonyms=yfiG; OrderedLocusNames=b2582, JW2566;
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 CHARACTERIZATION.
RC STRAIN=K12 / TG1;
RX PubMed=9388228; DOI=10.1074/jbc.272.49.30841;
RA Miranda-Vizuete A., Damdimopoulos A.E., Gustafsson J.-A., Spyrou G.;
RT "Cloning, expression, and characterization of a novel Escherichia coli
RT thioredoxin.";
RL J. Biol. Chem. 272:30841-30847(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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], AND SEQUENCE REVISION.
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 37-104.
RC STRAIN=K12;
RA Nashimoto H.;
RT "Non-ribosomal proteins affecting the assembly of ribosomes in Escherichia
RT coli.";
RL (In) Nierhaus K.H. (eds.);
RL The translational apparatus, pp.185-195, Plenum Press, New York (1993).
RN [6]
RP IDENTIFICATION.
RA Rudd K.E.;
RL Unpublished observations (NOV-1993).
CC -!- FUNCTION: Efficient electron donor for the essential enzyme
CC ribonucleotide reductase. Is also able to reduce the interchain
CC disulfide bridges of insulin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC -!- INTERACTION:
CC P0AGG4; P14900: murD; NbExp=2; IntAct=EBI-549392, EBI-554780;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; U85942; AAB88587.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75635.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16469.2; -; Genomic_DNA.
DR EMBL; D13169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; E65036; E65036.
DR RefSeq; NP_417077.1; NC_000913.3.
DR RefSeq; WP_001098726.1; NZ_STEB01000011.1.
DR AlphaFoldDB; P0AGG4; -.
DR SMR; P0AGG4; -.
DR BioGRID; 4263420; 20.
DR BioGRID; 851399; 2.
DR DIP; DIP-48115N; -.
DR IntAct; P0AGG4; 26.
DR STRING; 511145.b2582; -.
DR jPOST; P0AGG4; -.
DR PaxDb; P0AGG4; -.
DR PRIDE; P0AGG4; -.
DR EnsemblBacteria; AAC75635; AAC75635; b2582.
DR EnsemblBacteria; BAA16469; BAA16469; BAA16469.
DR GeneID; 67416962; -.
DR GeneID; 947062; -.
DR KEGG; ecj:JW2566; -.
DR KEGG; eco:b2582; -.
DR PATRIC; fig|1411691.4.peg.4152; -.
DR EchoBASE; EB1833; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_090389_10_0_6; -.
DR InParanoid; P0AGG4; -.
DR OMA; QRVDMIN; -.
DR PhylomeDB; P0AGG4; -.
DR BioCyc; EcoCyc:RED-THIOREDOXIN2-MON; -.
DR BioCyc; MetaCyc:RED-THIOREDOXIN2-MON; -.
DR PRO; PR:P0AGG4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IMP:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IMP:CACAO.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IMP:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01068; thioredoxin; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; Electron transport; Metal-binding; NAD;
KW Oxidoreductase; Redox-active center; Reference proteome; Transport; Zinc;
KW Zinc-finger.
FT CHAIN 1..139
FT /note="Thioredoxin 2"
FT /id="PRO_0000120102"
FT DOMAIN 26..139
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ZN_FING 5..18
FT /evidence="ECO:0000255"
FT DISULFID 64..67
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 139 AA; 15555 MW; 4C973F6FE55C8856 CRC64;
MNTVCTHCQA INRIPDDRIE DAAKCGRCGH DLFDGEVINA TGETLDKLLK DDLPVVIDFW
APWCGPCRNF APIFEDVAQE RSGKVRFVKV NTEAERELSS RFGIRSIPTI MIFKNGQVVD
MLNGAVPKAP FDSWLNESL
