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Database: UniProt
Entry: J4WLD5_9FIRM
LinkDB: J4WLD5_9FIRM
Original site: J4WLD5_9FIRM 
ID   J4WLD5_9FIRM            Unreviewed;       312 AA.
AC   J4WLD5;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Putative thioredoxin-disulfide reductase {ECO:0000313|EMBL:EJU25646.1};
GN   ORFNames=HMPREF1153_1401 {ECO:0000313|EMBL:EJU25646.1};
OS   Selenomonas sp. CM52.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=936381 {ECO:0000313|EMBL:EJU25646.1, ECO:0000313|Proteomes:UP000003116};
RN   [1] {ECO:0000313|EMBL:EJU25646.1, ECO:0000313|Proteomes:UP000003116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM52 {ECO:0000313|EMBL:EJU25646.1,
RC   ECO:0000313|Proteomes:UP000003116};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2012) 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:EJU25646.1}.
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DR   EMBL; ALNM01000046; EJU25646.1; -; Genomic_DNA.
DR   RefSeq; WP_009647016.1; NZ_ALNM01000046.1.
DR   AlphaFoldDB; J4WLD5; -.
DR   PATRIC; fig|936381.3.peg.2158; -.
DR   Proteomes; UP000003116; 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   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          8..294
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   312 AA;  33618 MW;  27DFE3860ACA953C CRC64;
     MAKETIQKDV VIIGAGMAGL TAALYAGRMN FSTLVLENAV VGGQIANATG IENYPGFLSV
     SGSDLIQTVQ QQAETFGAVV DEFDAIEKVT LEGAVKRVET ESAVYETPVV IIASGMSRRK
     LPLAEEAKYA GRGVHYCQLC DGHMYQDKII AVMGGGNAAL DAANFLSRYA KKLYLVHRSK
     LRADEVSQKR LRENPKAEIL LETEIRALRG EGKLESIEIF DKKAGEAREL AVDAIFVNIG
     VQPNTALFEG QVEINEKGHI VAGEDCRTNI PGVFVAGDIR EKEIHQLTTA ASDGTTAALL
     AEKYITGGKT SW
//
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