ID A0A1M7CYS5_9FLAO Unreviewed; 315 AA.
AC A0A1M7CYS5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN ORFNames=SAMN05443634_11620 {ECO:0000313|EMBL:SHL72388.1};
OS Chishuiella changwenlii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chishuiella.
OX NCBI_TaxID=1434701 {ECO:0000313|EMBL:SHL72388.1, ECO:0000313|Proteomes:UP000184120};
RN [1] {ECO:0000313|Proteomes:UP000184120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27989 {ECO:0000313|Proteomes:UP000184120};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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|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|RuleBase:RU003880}.
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DR EMBL; FRBH01000016; SHL72388.1; -; Genomic_DNA.
DR RefSeq; WP_072934062.1; NZ_FRBH01000016.1.
DR AlphaFoldDB; A0A1M7CYS5; -.
DR STRING; 1434701.SAMN05443634_11620; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000184120; Unassembled WGS sequence.
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 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 InterPro; IPR005982; Thioredox_Rdtase.
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 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 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 7..297
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 315 AA; 34112 MW; 5FDE94BC1F156AD9 CRC64;
MENNVRDVII IGSGPAGYTA GIYAARANMS PLILTGMEPG GQLTTTTEVE NFPGYPESIT
GPELMADLQK QAERFGTEIK YEYVTEVIFG DKQGDTHTVK TNIAEYVAKS IVISTGATAK
YLGLDDEKKY AGSGVSACAT CDGFFYRGKD VAVVGGGDTA AEEATYLAKL CKKVYLLVRK
DEMRASKAMQ HRVEHTANLE VLYHHELIGL EGNNVVEKAK IIDNQSNEEK ELIVDGVFIA
IGHKPNTDLF KGKLVMDETG YLITQDRSYS TNIPGVFAAG DVQDSVYRQA ITAAGSGCAA
ALDAERYVAE FFEEV
//
