GenomeNet

Database: UniProt/SWISS-PROT
Entry: THIO2_SHIFL
LinkDB: THIO2_SHIFL
Original site: THIO2_SHIFL 
ID   THIO2_SHIFL             Reviewed;         139 AA.
AC   P0AGG7; P33636; P76593; P77000; P77001;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   11-JUN-2014, entry version 66.
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=SF2644, S2817;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN44140.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17964.1; -; Genomic_DNA.
DR   RefSeq; NP_708433.1; NC_004337.2.
DR   RefSeq; NP_838154.1; NC_004741.1.
DR   ProteinModelPortal; P0AGG7; -.
DR   STRING; 198214.SF2644; -.
DR   PaxDb; P0AGG7; -.
DR   EnsemblBacteria; AAN44140; AAN44140; SF2644.
DR   EnsemblBacteria; AAP17964; AAP17964; S2817.
DR   GeneID; 1026952; -.
DR   GeneID; 1079081; -.
DR   KEGG; sfl:SF2644; -.
DR   KEGG; sfx:S2817; -.
DR   PATRIC; 18707283; VBIShiFle31049_3109.
DR   eggNOG; COG0526; -.
DR   HOGENOM; HOG000292979; -.
DR   KO; K03672; -.
DR   OMA; RVDMING; -.
DR   OrthoDB; EOG6QG8RK; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0047134; F:protein-disulfide reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.30.10; -; 1.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10438; PTHR10438; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; 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   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_0000120105.
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
//
DBGET integrated database retrieval system