UniProt: G8PC18

Database: UniProt
Entry: G8PC18_PEDCP

LinkDB:  G8PC18_PEDCP 
Original site:  G8PC18_PEDCP

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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   G8PC18_PEDCP            Unreviewed;       312 AA.
AC   G8PC18;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Thioredoxin reductase {ECO:0000256|ARBA:ARBA00018719, ECO:0000256|RuleBase:RU003880};
DE            EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN   Name=trxB {ECO:0000313|EMBL:AEV94837.1};
GN   OrderedLocusNames=PECL_536 {ECO:0000313|EMBL:AEV94837.1};
OS   Pediococcus claussenii (strain ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC
OS   3811 / P06).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=701521 {ECO:0000313|EMBL:AEV94837.1, ECO:0000313|Proteomes:UP000005444};
RN   [1] {ECO:0000313|Proteomes:UP000005444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC   {ECO:0000313|Proteomes:UP000005444};
RA   Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA   Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA   Kusalik A., Ziola B.;
RT   "Genome and plasmid sequences for the beer-spoilage organism Pediococcus
RT   claussenii ATCC BAA-344T.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV94837.1, ECO:0000313|Proteomes:UP000005444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC   {ECO:0000313|Proteomes:UP000005444};
RX   PubMed=22328764; DOI=10.1128/JB.06759-11;
RA   Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA   Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA   Kusalik A., Ziola B.;
RT   "Complete Genome Sequence of the Beer Spoilage Organism Pediococcus
RT   claussenii ATCC BAA-344T.";
RL   J. Bacteriol. 194:1271-1272(2012).
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|ARBA:ARBA00011738,
CC       ECO:0000256|RuleBase:RU003880}.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333,
CC       ECO:0000256|RuleBase:RU003880}.
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DR   EMBL; CP003137; AEV94837.1; -; Genomic_DNA.
DR   RefSeq; WP_014215034.1; NC_016605.1.
DR   AlphaFoldDB; G8PC18; -.
DR   STRING; 701521.PECL_536; -.
DR   KEGG; pce:PECL_536; -.
DR   PATRIC; fig|701521.8.peg.514; -.
DR   eggNOG; COG0492; Bacteria.
DR   HOGENOM; CLU_031864_5_3_9; -.
DR   Proteomes; UP000005444; 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:UP000005444}.
FT   DOMAIN          5..292
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   312 AA;  33713 MW;  5E811CC3FEC43742 CRC64;
     MAKEYDIIII GAGPAGMTAA LYASRANMSV LMLDRGIYGG QMNNTASIEN YPGFKSILGP
     DLAKEMYDSS TQFGAEYSYG SVESVVNDGD TKTITTDMGD EFITKVLIIG TGSEYKKLGV
     PGEEDFSGRG VSYCAVCDGA FFKGMHLVVI GGGDSAIEEG IYLTQLASKV TVIHRRDQLR
     AQKITQQRAF DNDKMEFVWN SNVTEIVGDD KVEGVKVNNN KTGEDSFIDA SGVFIYVGVQ
     PMTAPFKGLG ILDEDGWIPT DELMHTKVPG IFAVGDVRKK NLRQIATAVG EGGTAAQQAF
     DYIQEINSKQ NV
//

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