ID   THIO_HAEIN              Reviewed;         107 AA.
AC   P43785;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA; Synonyms=trxM; OrderedLocusNames=HI_0084;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Participates in various redox reactions through the
CC       reversible oxidation of its active center dithiol to a disulfide and
CC       catalyzes dithiol-disulfide exchange reactions. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; L42023; AAC21757.1; -; Genomic_DNA.
DR   PIR; E64047; E64047.
DR   RefSeq; NP_438257.1; NC_000907.1.
DR   RefSeq; WP_005693835.1; NC_000907.1.
DR   AlphaFoldDB; P43785; -.
DR   SMR; P43785; -.
DR   STRING; 71421.HI_0084; -.
DR   EnsemblBacteria; AAC21757; AAC21757; HI_0084.
DR   KEGG; hin:HI_0084; -.
DR   PATRIC; fig|71421.8.peg.85; -.
DR   eggNOG; COG3118; Bacteria.
DR   HOGENOM; CLU_090389_10_2_6; -.
DR   OMA; QVGVAPK; -.
DR   PhylomeDB; P43785; -.
DR   BioCyc; HINF71421:G1GJ1-85-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
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   Disulfide bond; Electron transport; Redox-active center;
KW   Reference proteome; Transport.
FT   CHAIN           1..107
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120107"
FT   DOMAIN          2..107
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        32..35
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   107 AA;  11681 MW;  1725C8A244685477 CRC64;
     MSEVLHINDA DFESVVVNSD IPILLDFWAP WCGPCKMIAP VLDELAPEFA GKVKIVKMNV
     DDNQATPAQF GVRSIPTLLL IKNGQVVATQ VGALPKTQLA NFINQHI