ID A0A0C5BBJ2_9MOLU Unreviewed; 309 AA.
AC A0A0C5BBJ2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN Name=trxB {ECO:0000313|EMBL:AJM71960.1};
GN ORFNames=MYE_02435 {ECO:0000313|EMBL:AJM71960.1};
OS Mycoplasma yeatsii GM274B.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=743967 {ECO:0000313|EMBL:AJM71960.1, ECO:0000313|Proteomes:UP000032020};
RN [1] {ECO:0000313|EMBL:AJM71960.1, ECO:0000313|Proteomes:UP000032020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM274B {ECO:0000313|EMBL:AJM71960.1,
RC ECO:0000313|Proteomes:UP000032020};
RX PubMed=25908137; DOI=10.1128/genomeA.00328-15;
RA Calcutt M.J., Kent B.N., Foecking M.F.;
RT "Complete genome sequence of Mycoplasma yeatsii strain GM274B (ATCC
RT 43094).";
RL Genome Announc. 3:0-0(2015).
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 ---------------------------------------------------------------------------
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; CP007520; AJM71960.1; -; Genomic_DNA.
DR RefSeq; WP_042733382.1; NZ_CP007520.1.
DR AlphaFoldDB; A0A0C5BBJ2; -.
DR STRING; 743967.MYE_02435; -.
DR KEGG; myt:MYE_02435; -.
DR PATRIC; fig|743967.3.peg.481; -.
DR HOGENOM; CLU_031864_5_3_14; -.
DR Proteomes; UP000032020; 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; 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..290
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 309 AA; 33461 MW; 3729FD55C043733E CRC64;
MKNLTNEVYD VLIVGAGPAG LTAAIYTTRA GLKTVVFEHS APGGKLVKTD LIENYPGFET
ITGPDLAMKM YMQATSLGAE IQFYGVSKIT KNEDLFEVEL SNGEIKKAIS VILASGTEEN
KLGIPGEDKL YGKGVSYCAV CDGAFYKNKP VAVVGGGYSA VQEAMYLSQL VDKVYLIVRR
DVFRADANKV AKLKAQNNVE FILKSQVKQI NGEEKVESIL VNTPEGEKTI KVDAIFPYIG
STPVIESVKD LHLENEKGYI PTTDKMESTI KGLYIAGDVR DVPLRQIAIA CGDGAIAGQM
AVEYVQEVK
//
