ID THIO2_ECO57 Reviewed; 139 AA. AC P0AGG6; 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 29. 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=Z3867, ECs3448; OS Escherichia coli O157:H7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX MEDLINE=21074935; PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., RA Welch R.A., Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX MEDLINE=21156231; PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., RA Kuhara S., Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli RT O157:H7 and genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). 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; AE005174; AAG57699.1; -; Genomic_DNA. DR EMBL; BA000007; BAB36871.1; -; Genomic_DNA. DR PIR; G85904; G85904. DR PIR; H91059; H91059. DR RefSeq; NP_289141.1; -. DR RefSeq; NP_311475.1; -. DR HSSP; P23400; 1DBY. DR GeneID; 914878; -. DR GeneID; 957981; -. DR GenomeReviews; AE005174_GR; Z3867. DR GenomeReviews; BA000007_GR; ECs3448. DR KEGG; ece:Z3867; -. DR KEGG; ecs:ECs3448; -. DR HOGENOM; P0AGG6; -. DR OMA; P0AGG6; MIFKQGH. DR BioCyc; ECOL83334:ECS3448-MON; -. 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_0000120103. 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 //