ID   THIO2_ECOL6             Reviewed;         139 AA.
AC   P0AGG5; 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; OrderedLocusNames=c3107;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Efficient electron donor for the essential enzyme
CC       ribonucleotide reductase. Is also able to reduce the interchain
CC       disulfide bridges of insulin (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein dithiol + NAD(P)(+) = protein
CC       disulfide + NAD(P)H.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE014075; AAN81556.1; -; Genomic_DNA.
DR   RefSeq; NP_754988.1; -.
DR   HSSP; P23400; 1DBY.
DR   GeneID; 1038821; -.
DR   GenomeReviews; AE014075_GR; c3107.
DR   KEGG; ecc:c3107; -.
DR   HOGENOM; P0AGG5; -.
DR   OMA; P0AGG5; MIFKQGH.
DR   BRENDA; 1.8.1.8; 292881.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
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   3: Inferred from homology;
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_0000120104.
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
//