UniProt: A0A060JEB5

Database: UniProt
Entry: A0A060JEB5_9MICO

LinkDB:  A0A060JEB5_9MICO 
Original site:  A0A060JEB5_9MICO

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (14)   

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ID   A0A060JEB5_9MICO        Unreviewed;       306 AA.
AC   A0A060JEB5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE            EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN   ORFNames=Rhola_00013970 {ECO:0000313|EMBL:AIC48186.1};
OS   Rhodoluna lacicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Luna cluster; Luna-1 subcluster; Rhodoluna.
OX   NCBI_TaxID=529884 {ECO:0000313|EMBL:AIC48186.1, ECO:0000313|Proteomes:UP000067708};
RN   [1] {ECO:0000313|EMBL:AIC48186.1, ECO:0000313|Proteomes:UP000067708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWH-Ta8 {ECO:0000313|EMBL:AIC48186.1,
RC   ECO:0000313|Proteomes:UP000067708};
RX   PubMed=24984700; DOI=10.1099/ijs.0.065292-0;
RA   Hahn M., Schmidt J., Taipale S.J., Doolittle W.F., Koll U.;
RT   "Rhodoluna lacicola gen. nov., sp. nov., a planktonic freshwater bacterium
RT   with stream-lined genome.";
RL   Int. J. Syst. Evol. Microbiol. 64:3254-3263(2014).
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|ARBA:ARBA00000849,
CC         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; CP007490; AIC48186.1; -; Genomic_DNA.
DR   RefSeq; WP_038503445.1; NZ_CP007490.1.
DR   AlphaFoldDB; A0A060JEB5; -.
DR   STRING; 529884.Rhola_00013970; -.
DR   KEGG; rla:Rhola_00013970; -.
DR   PATRIC; fig|529884.3.peg.1356; -.
DR   eggNOG; COG0492; Bacteria.
DR   HOGENOM; CLU_031864_5_1_11; -.
DR   OrthoDB; 9806179at2; -.
DR   Proteomes; UP000067708; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067708}.
FT   DOMAIN          3..292
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   306 AA;  32919 MW;  378AE911B392C315 CRC64;
     MRDVIIIGSG PAGYTAGIYT ARAGLKPLLI ASSVEAGGEL MKTTEVENYP GFPEGLMGPE
     LMAHFQAQAE RFGTEILMDD VVEVDLKGDV KIVKTGAGET FEAKTVILAT GAAYRELGLP
     REKELSGHGV SWCATCDGFF FREKTIAVVG GGDSAMEEAL FLTRFASKVY LIHRRDTFKA
     SKIMQDRALA HEKIEVIWNS EVAELKGEKN LEGVTLKSTV DGSTSELALD GLFIAVGNDP
     RVWLVEDQVT LTPEKFIQVE GRSSKTNLPG VFACGDVIDP TYRQAITAAG SGCVAALDAE
     HFLANH
//

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