ID   A0A101VWA1_9FIRM        Unreviewed;       404 AA.
AC   A0A101VWA1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KUO62052.1};
GN   ORFNames=APF84_07735 {ECO:0000313|EMBL:KUO62052.1};
OS   Gracilibacter sp. BRH_c7a.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Gracilibacteraceae;
OC   Gracilibacter.
OX   NCBI_TaxID=1734398 {ECO:0000313|EMBL:KUO62052.1, ECO:0000313|Proteomes:UP000053404};
RN   [1] {ECO:0000313|EMBL:KUO62052.1, ECO:0000313|Proteomes:UP000053404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c7a {ECO:0000313|EMBL:KUO62052.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333}.
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:KUO62052.1}.
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DR   EMBL; LOEZ01000060; KUO62052.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101VWA1; -.
DR   STRING; 1734398.APF84_07735; -.
DR   Proteomes; UP000053404; Unassembled WGS sequence.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:UniProt.
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; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT   DOMAIN          5..295
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          308..397
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00085"
SQ   SEQUENCE   404 AA;  44948 MW;  7CDA164C7307C737 CRC64;
     MVNLYDLVII GAGPAGLSAA IYGGRAKLST LVINKGRVGG LVNTTREIVN YPGYRQINGE
     GLMKDFKKHA ESFGVEFISD EVVSTNYLKE NKIIRTKKGN VYKAKAVINA CGSQPRLLNI
     PGEKRLQGSG VAYCATCDAE FFEGEDVVVI GSGDQAIEEG IYITKFARKV TVTVLHEEGI
     LDCNKVSAER AFQNEKMEFI WNSTIEEVLG EEKVEGVKIM NLKTGCSTEL ICQGVFFFVG
     MVPSTHFLKD GGIAMDERGY ILVNELMETN LEGVYAVGDN RTKYLRQVVT AAGDGAIAAV
     AAERYIEEQN EFNMKVIQSD KKVLLLFFNA TEDESLKFST LLEEINREMD EYYRVIKIDM
     ATKKNLAKKY RIESAPSVVV LDRGQEVKRL KCLMDKEIIK CQLL
//