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 01-MAY-2013, entry version 61.
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.
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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 SMR; P0AGG7; 1-139.
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; IVCPHCH; -.
DR ProtClustDB; PRK10996; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
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:EC.
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 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 PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thiordxn-like_fd; 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
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