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   16-JUN-2009, entry version 31.
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; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=K12 / TG1;
RX   MEDLINE=98049550; 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   MEDLINE=97349980; PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA   Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA   Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA   Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA   Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA   Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT   K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT   analysis of 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   MEDLINE=97426617; 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], 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
RT   MG1655 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
RT   Escherichia coli.";
RL   (In) Nierhaus K.H. (eds.);
RL   The translational apparatus, pp.185-195, Plenum Press, New York
RL   (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: Protein dithiol + NAD(P)(+) = protein
CC       disulfide + NAD(P)H.
CC   -!- INTERACTION:
CC       P14900:murD; NbExp=1; IntAct=EBI-549392, EBI-554780;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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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; AP_003168.1; -.
DR   RefSeq; NP_417077.1; -.
DR   HSSP; P23400; 1DBY.
DR   IntAct; P0AGG4; 23.
DR   GeneID; 947062; -.
DR   GenomeReviews; AP009048_GR; JW2566.
DR   GenomeReviews; U00096_GR; b2582.
DR   KEGG; ecj:JW2566; -.
DR   KEGG; eco:b2582; -.
DR   EchoBASE; EB1833; -.
DR   EcoGene; EG11887; trxC.
DR   HOGENOM; P0AGG4; -.
DR   OMA; P0AGG4; MIFKQGH.
DR   BioCyc; EcoCyc:RED-THIOREDOXIN2-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0047134; F:protein-disulfide reductase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR006662; Thioredoxin-like_subdom.
DR   InterPro; IPR015467; Thioredoxin_core.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   PANTHER; PTHR10438; Trx; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   TIGRFAMs; TIGR01068; thioredoxin; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Disulfide bond; Electron transport;
KW   Metal-binding; NAD; Oxidoreductase; Redox-active center; Transport;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    139       Thioredoxin-2.
FT                                /FTId=PRO_0000120102.
FT   DOMAIN       26    139       Thioredoxin.
FT   ZN_FING       5     18       Potential.
FT   DISULFID     64     67       Redox-active (By similarity).
SQ   SEQUENCE   139 AA;  15555 MW;  4C973F6FE55C8856 CRC64;
     MNTVCTHCQA INRIPDDRIE DAAKCGRCGH DLFDGEVINA TGETLDKLLK DDLPVVIDFW
     APWCGPCRNF APIFEDVAQE RSGKVRFVKV NTEAERELSS RFGIRSIPTI MIFKNGQVVD
     MLNGAVPKAP FDSWLNESL
//