ID A0A3R9YLI3_9ENTE Unreviewed; 317 AA.
AC A0A3R9YLI3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Thioredoxin-disulfide reductase {ECO:0000313|EMBL:RST90459.1};
GN ORFNames=C7P63_03550 {ECO:0000313|EMBL:RST90459.1};
OS Vagococcus humatus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=1889241 {ECO:0000313|EMBL:RST90459.1, ECO:0000313|Proteomes:UP000277864};
RN [1] {ECO:0000313|EMBL:RST90459.1, ECO:0000313|Proteomes:UP000277864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 31581 {ECO:0000313|EMBL:RST90459.1,
RC ECO:0000313|Proteomes:UP000277864};
RA Gulvik C.A.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:RST90459.1}.
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DR EMBL; PXZH01000001; RST90459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9YLI3; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000277864; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000277864}.
FT DOMAIN 2..302
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 317 AA; 33923 MW; E61E226D8FDED81B CRC64;
MYDVVIIGGG PAGLTAALYN ARARLKVIVL EKTKLGGQIV TTHEIANFPG SVVGSSEEEP
SGPELIKRMT DQAKKYGAQI EVGKEVVGLD LDGDVKTITC QDGTTYQSLA VICANGASPR
KIGCPGEAEL QGKGVSYCAT CDGAFFEDME IYVIGGGNSA VEEATFLTSF GRKVHIIQNL
DRLTADAIAI EQAKKSGKID VTYNTVVEEI KGDGLVESMV LKNTETGEVT EVFADEEDGT
FGVFVFIGYI PTTTLYQDKL ELNEWGYIQT NECMETSIKG VFAAGDIRPK LLRQVVTATG
DGATAAFAVQ KYVESKR
//
