ID A0A085EEY5_9FLAO Unreviewed; 324 AA.
AC A0A085EEY5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN ORFNames=FEM08_34380 {ECO:0000313|EMBL:KFC57780.1};
OS Flavobacterium gilvum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1492737 {ECO:0000313|EMBL:KFC57780.1, ECO:0000313|Proteomes:UP000028636};
RN [1] {ECO:0000313|EMBL:KFC57780.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM1308 {ECO:0000313|EMBL:KFC57780.1};
RA Shin S.-K., Yi H.;
RT "Genome Sequence of Flavobacterium sp. EM1308.";
RL Submitted (MAY-2014) 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}.
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:KFC57780.1}.
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DR EMBL; JNCP01000143; KFC57780.1; -; Genomic_DNA.
DR RefSeq; WP_035640823.1; NZ_JNCP01000143.1.
DR AlphaFoldDB; A0A085EEY5; -.
DR STRING; 1492737.EM308_08510; -.
DR KEGG; fgl:EM308_08510; -.
DR PATRIC; fig|1492737.3.peg.3420; -.
DR eggNOG; COG0492; Bacteria.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000028636; 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}.
FT DOMAIN 9..300
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 324 AA; 35045 MW; 15AD20EEB034086C CRC64;
MSDTIEKIKC LIIGSGPAGY TAAIYAARAN MNPVLYQGMQ PGGQLTTTNE VENFPGYVDG
VTGPEMMIQL QQQAQRFGAD VRDGWATKVD FSGDIHKVWI NDKIELHCET VIISTGASAK
YLGLESEQHY LKMGGGVSAC AVCDGFFYRN QEVVIVGAGD SACEEAHYLS KLCSKVTMLV
RSDKFRASKI MEARVRKTEN ISILMNHDTV EILGDGQVVN GVKAKNKTTG EIFDIPATGF
FAAIGHKPNT DIFRDYLTLD ETGYIINVPG TSKTNVEGVF VAGDAADHVY RQAITAAGTG
CMAALDAERY LAAKESEVEE KVIS
//
