ID A0A1H6YL72_9BACT Unreviewed; 322 AA.
AC A0A1H6YL72;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN ORFNames=SAMN04487995_4607 {ECO:0000313|EMBL:SEJ42019.1};
OS Dyadobacter koreensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=408657 {ECO:0000313|EMBL:SEJ42019.1, ECO:0000313|Proteomes:UP000199532};
RN [1] {ECO:0000313|EMBL:SEJ42019.1, ECO:0000313|Proteomes:UP000199532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19938 {ECO:0000313|EMBL:SEJ42019.1,
RC ECO:0000313|Proteomes:UP000199532};
RA de Groot N.N.;
RL Submitted (OCT-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:RU003880};
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; FNXY01000007; SEJ42019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6YL72; -.
DR STRING; 408657.SAMN04487995_4607; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000199532; 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; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003880};
KW Flavoprotein {ECO:0000256|RuleBase:RU003880};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003880};
KW Redox-active center {ECO:0000256|RuleBase:RU003880};
KW Reference proteome {ECO:0000313|Proteomes:UP000199532}.
FT DOMAIN 7..295
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 322 AA; 34926 MW; C92BF0A9F88CC7C7 CRC64;
MTSEKVDCLI IGSGPAGYTA AIYASRAGLN PVLYQGAQPG GQLTITTEVD NYPGYPDGIT
GPEMMINFEK QAKRFGADIR YGMATAVDFT SYPRKVIIDG QKEILADAVI ISTGASAKWL
GLEDEERLNG HGVSACAVCD GFFFRNQDVV VVGAGDTAAE EASYLAKLCR KVYLVVRRDE
MRASKIMQKR LETLPNIEIL WNTETVKLNG EEGLESVLVK NNKTGEETLL DVTGFFVAIG
HKPNTDIFKG YIDMDETGYI KTVKGSAHTN VSGVFACGDA QDNVYRQAIT AAGTGCMAAL
DAERFLMERE VEIIADDILE TN
//