ID   TRXB_PNEJI              Reviewed;         327 AA.
AC   Q8J0U0;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Thioredoxin reductase;
DE            EC=1.8.1.9;
GN   Name=TRR1;
OS   Pneumocystis jiroveci.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis.
OX   NCBI_TaxID=42068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=22686537; PubMed=12801645; DOI=10.1016/S0378-1119(03)00549-3;
RA   Kutty G.K., Huang S.N., Kovacs J.A.;
RT   "Characterization of thioredoxin reductase genes (trr1) from
RT   Pneumocystis carinii and Pneumocystis jiroveci.";
RL   Gene 310:175-183(2003).
CC   -!- FUNCTION: Component of the thioredoxin-thioredoxin reductase
CC       system which may be involved in biosynthesis of penicillins and
CC       cephalosporins and may be important in determining the thiol-
CC       disulfide redox balance.
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; AY130996; AAN12366.1; -; Genomic_DNA.
DR   EMBL; AF532986; AAP72145.1; -; mRNA.
DR   HSSP; Q39243; 1VDC.
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   2: Evidence at transcript level;
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN         1    327       Thioredoxin reductase.
FT                                /FTId=PRO_0000166767.
FT   NP_BIND      32     44       FAD (By similarity).
FT   NP_BIND     286    295       FAD (By similarity).
FT   DISULFID    140    143       Redox-active (By similarity).
SQ   SEQUENCE   327 AA;  35608 MW;  6A5D230F87BF5777 CRC64;
     MHSKVIIIGS GPAGHTAAIY LARAELKPVL YEGMLANGIA AGGQLTTTTD VENYPGFPDG
     IMGPLLMEKF REQSVKYGTC IITETVSKLD LSKRPFKYWC ESDENTCHTA DVVVMATGAY
     ARRLHIPGEE TYWQRGISAC AVCDGAAPIF RGKCLSVVGG GDSAAEESLF LTRYATKVYL
     LVRRDKLRAS AVMAKRLLNH PKIEVIWNTV VLRSLGDGHL LNRLEIKNVK TQVVSELHVS
     GLFYAIGHEP ATALVRGQVE CDDNGYIITK NGGPETNIKG FFAAGDVQDK KWRQAVTSAG
     SGCMAGLAAE RLLAEEEEMK NIEKNKK
//