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Database: UniProt
Entry: I4D909_DESAJ
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ID   I4D909_DESAJ            Unreviewed;       407 AA.
AC   I4D909;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE            EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN   OrderedLocusNames=Desaci_3389 {ECO:0000313|EMBL:AFM42283.1};
OS   Desulfosporosinus acidiphilus (strain DSM 22704 / JCM 16185 / SJ4).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=646529 {ECO:0000313|EMBL:AFM42283.1, ECO:0000313|Proteomes:UP000002892};
RN   [1] {ECO:0000313|EMBL:AFM42283.1, ECO:0000313|Proteomes:UP000002892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22704 / JCM 16185 / SJ4
RC   {ECO:0000313|Proteomes:UP000002892};
RX   PubMed=23105050; DOI=10.1128/JB.01392-12;
RA   Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA   Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA   Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA   Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA   Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA   Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA   Ollivier B., Klenk H.P., Spring S., Loy A.;
RT   "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT   Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT   and Desulfosporosinus acidiphilus DSM22704T.";
RL   J. Bacteriol. 194:6300-6301(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC         H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC         Evidence={ECO:0000256|RuleBase:RU003880};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU003881};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003881};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU003880}.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333,
CC       ECO:0000256|RuleBase:RU003880}.
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DR   EMBL; CP003639; AFM42283.1; -; Genomic_DNA.
DR   RefSeq; WP_014828272.1; NC_018068.1.
DR   AlphaFoldDB; I4D909; -.
DR   STRING; 646529.Desaci_3389; -.
DR   KEGG; dai:Desaci_3389; -.
DR   eggNOG; COG0492; Bacteria.
DR   HOGENOM; CLU_031864_5_3_9; -.
DR   OMA; HEMENYP; -.
DR   OrthoDB; 9806179at2; -.
DR   Proteomes; UP000002892; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:UniProtKB-UniRule.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01292; TRX_reduct; 1.
DR   PANTHER; PTHR48105:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 1.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|RuleBase:RU003880};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003880};
KW   NADP {ECO:0000256|RuleBase:RU003881};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003880};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003880}.
FT   DOMAIN          8..298
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          312..405
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00085"
SQ   SEQUENCE   407 AA;  44567 MW;  F08B6B244D4E729E CRC64;
     MGDITSTYDL IIVGGGPAGL SAAIYGGRAK LKTLVINKGT VGGLVNTTRE IVNYPGYGQI
     SGEDLMKDFK KHAESFGTEF LRDEVIRTDF SQEDKVITTK KGKVFSAKAV IIACGSEPRL
     LNIPGEKRLQ GSGVAYCATC DAEFFEGEDV VVVGSGDQAI EEGMYITKFA RKVTVIVLHD
     EGILDCNKVS AERAFQNPKM EFIWNSTLEE VQGQDNVEGV KIKNLKTGAS TELACQGVFF
     FVGMVPSTHF LKESGIEIDK RGYIPVNELM ETNLEGVYAV GDNRVKYLRQ VVSAAGDGAT
     AAVAAERYIE EMKAFNVNVL ESDKQVLLLF FNALDNRSLE FGTSLEEVNK ELLERYKIVN
     VDLTTKRSLA QKYGIEKAPS VVVLDKGQEV KRLDCSTTIE NLKSQVC
//
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