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Database: UniProt
Entry: A0A1H6YL72_9BACT
LinkDB: A0A1H6YL72_9BACT
Original site: A0A1H6YL72_9BACT 
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
//
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