ID   TRXB_HAEIN              Reviewed;         318 AA.
AC   P43788;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-JUN-2009, entry version 72.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB; OrderedLocusNames=HI1158;
OS   Haemophilus influenzae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   MEDLINE=95350630; 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.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide
CC       + NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; L42023; AAC22813.1; -; Genomic_DNA.
DR   PIR; G64186; G64186.
DR   RefSeq; NP_439316.1; -.
DR   HSSP; P09625; 1TRB.
DR   SMR; P43788; 5-315.
DR   GeneID; 950118; -.
DR   GenomeReviews; L42023_GR; HI1158.
DR   KEGG; hin:HI1158; -.
DR   NMPDR; fig|71421.1.peg.1111; -.
DR   TIGR; HI1158; -.
DR   HOGENOM; P43788; -.
DR   OMA; P43788; PSCGPCH.
DR   BioCyc; HINF71421:HI_1158-MON; -.
DR   BRENDA; 1.8.1.9; 109.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP;
KW   Oxidoreductase; Redox-active center.
FT   CHAIN         1    318       Thioredoxin reductase.
FT                                /FTId=PRO_0000166732.
FT   NP_BIND      36     43       FAD (By similarity).
FT   NP_BIND     286    295       FAD (By similarity).
FT   DISULFID    136    139       Redox-active (By similarity).
SQ   SEQUENCE   318 AA;  34395 MW;  2BAEBC5DDE6020AA CRC64;
     MSDIKHAKLL ILGSGPAGYT AAIYAARANL KPVLVTGLQQ GGQLTTTDEI ENWPGDFEMT
     TGSGLMQRML QHAEKFETEI VFDHINRVDL SSRPFKLFGD VQNFTCDALI IATGASARYI
     GLPSEENYKG RGVSACATCD GFFYRNKPVG VIGGGNTAVE EALYLANIAS TVHLIHRRDS
     FRAEKILIDR LYKKVEEGKI VLHTDRTLDE VLGDNMGVTG LRLANTKTGE KEELKLDGLF
     VAIGHSPNTE IFQGQLELNN GYIVVKSGLD GNATATSVEG VFAAGDVMDH NYRQAITSAG
     TGCMAALDAE RYLDAQEA
//