ID   A0A133XS96_9ACTN        Unreviewed;       323 AA.
AC   A0A133XS96;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Putative thioredoxin-disulfide reductase {ECO:0000313|EMBL:KXB33798.1};
GN   ORFNames=HMPREF3192_01027 {ECO:0000313|EMBL:KXB33798.1};
OS   Atopobium deltae.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Atopobium.
OX   NCBI_TaxID=1393034 {ECO:0000313|EMBL:KXB33798.1, ECO:0000313|Proteomes:UP000070675};
RN   [1] {ECO:0000313|Proteomes:UP000070675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DNF00019 {ECO:0000313|Proteomes:UP000070675};
RA   Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA   O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA   Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000849};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXB33798.1}.
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DR   EMBL; LSCR01000029; KXB33798.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A133XS96; -.
DR   STRING; 1393034.HMPREF3192_01027; -.
DR   PATRIC; fig|1393034.3.peg.991; -.
DR   Proteomes; UP000070675; Unassembled WGS sequence.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
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   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070675}.
FT   DOMAIN          13..307
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   323 AA;  34229 MW;  2927CE82D1F8A3F6 CRC64;
     MLFGGVLVNT VYHDIIIVGA GPAGLAAAIY ATRAMSDALA LEQTAVGGQV ITTTDIDNYP
     GAPQTNGFEL MQSMEQQARD LGAQIQSDKI SAIEKNPSTQ LFELRSADDQ TLYTAKAVIY
     AAGATPRRAG FTNEQKFTGQ GISYCGTCDG MFYRGKTVFV VGGGNTAVEE ALFLTRFATQ
     VVMIVRKDHL RASQALIERL KTNEKVSIRY NTSIVAVHGE QLLTSIDFKD EKTAEISAQS
     FDEGSCGIFV FTGQTPASEA VKGLVELTDA GAIKTDVRLQ TKTAGLFAAG DVRDTPLRQI
     ITAAADGALA ASGAAAYVGS RME
//