UniProt: A0A090Z8R5

Database: UniProt
Entry: A0A090Z8R5_PAEMA

LinkDB:  A0A090Z8R5_PAEMA 
Original site:  A0A090Z8R5_PAEMA

All links

Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (6)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (1)   
All databases (14)   

Download RDF

ID   A0A090Z8R5_PAEMA        Unreviewed;       315 AA.
AC   A0A090Z8R5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
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:KFN07654.1};
GN   ORFNames=DJ90_6085 {ECO:0000313|EMBL:KFN07654.1}, GNQ08_07105
GN   {ECO:0000313|EMBL:MUG22188.1};
OS   Paenibacillus macerans (Bacillus macerans).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=44252 {ECO:0000313|EMBL:KFN07654.1, ECO:0000313|Proteomes:UP000029278};
RN   [1] {ECO:0000313|EMBL:KFN07654.1, ECO:0000313|Proteomes:UP000029278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8244 {ECO:0000313|EMBL:KFN07654.1,
RC   ECO:0000313|Proteomes:UP000029278};
RA   Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA   Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA   Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA   Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA   Scholz M.B., Teshima H., Xu Y.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MUG22188.1, ECO:0000313|Proteomes:UP000442469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3CT49 {ECO:0000313|EMBL:MUG22188.1,
RC   ECO:0000313|Proteomes:UP000442469};
RA   Olajide A.M., Chen S., Lapointe G.;
RT   "Draft genome sequences of five Paenibacillus species of dairy origin.";
RL   Submitted (NOV-2019) 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|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}.
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:KFN07654.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JMQA01000032; KFN07654.1; -; Genomic_DNA.
DR   EMBL; WNZZ01000004; MUG22188.1; -; Genomic_DNA.
DR   RefSeq; WP_036627158.1; NZ_WNZZ01000004.1.
DR   AlphaFoldDB; A0A090Z8R5; -.
DR   STRING; 44252.DJ90_6085; -.
DR   GeneID; 77010269; -.
DR   PATRIC; fig|44252.3.peg.3792; -.
DR   HOGENOM; CLU_031864_5_1_9; -.
DR   OrthoDB; 9806179at2; -.
DR   Proteomes; UP000029278; Unassembled WGS sequence.
DR   Proteomes; UP000442469; 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; 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:UP000029278}.
FT   DOMAIN          3..293
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   315 AA;  33821 MW;  7E6443A77BC3352F CRC64;
     MRKTMVIGTG PAGLTAAIYL ARANLSPIVI EGTQPGGQLT TTTEVENFPG FPEGIMGPEL
     MDNMRKQAER FGAEFRNGWV EGVDFSKRPF KVKLEGGEEL EAESVIISTG ASAKYLGIPG
     EQDNVGRGVS TCATCDGFFF RGKKILVIGG GDSAMEEANF LTRFATEVTV VHRREELRAS
     KIMQDRAKGN GKISWALNRT PLEVVTDETG TVKGLKVRNN ATGQEELLEA QGVFVAIGHT
     PNTKFLGGAV ETDDHGYILV KPGTTETNVP GVFACGDVQD MRYRQAITAA GSGCMAAMDC
     EKFLEGSMVH DWSGN
//

DBGET integrated database retrieval system