ID A0A0K1W092_9MOLU Unreviewed; 312 AA.
AC A0A0K1W092;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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:AKX33729.1};
GN ORFNames=SLITO_v1c00610 {ECO:0000313|EMBL:AKX33729.1};
OS Spiroplasma litorale.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=216942 {ECO:0000313|EMBL:AKX33729.1, ECO:0000313|Proteomes:UP000067476};
RN [1] {ECO:0000313|EMBL:AKX33729.1, ECO:0000313|Proteomes:UP000067476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN-1 {ECO:0000313|EMBL:AKX33729.1,
RC ECO:0000313|Proteomes:UP000067476};
RX PubMed=26430038;
RA Lo W.S., Lai Y.C., Lien Y.W., Wang T.H., Kuo C.H.;
RT "Complete Genome Sequence of Spiroplasma litorale TN-1T (DSM 21781), a
RT Bacterium Isolated from a Green-Eyed Horsefly (Tabanus nigrovittatus).";
RL Genome Announc. 3:e01116-15(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}.
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DR EMBL; CP012357; AKX33729.1; -; Genomic_DNA.
DR RefSeq; WP_075057830.1; NZ_CP012357.1.
DR AlphaFoldDB; A0A0K1W092; -.
DR STRING; 216942.SLITO_v1c00610; -.
DR KEGG; sll:SLITO_v1c00610; -.
DR PATRIC; fig|216942.3.peg.61; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000067476; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000067476}.
FT DOMAIN 9..297
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 312 AA; 34212 MW; E0B8794D769C8C00 CRC64;
MKNLIKTDYD LIIVGEGPAG LSAAIYSCRA GLRTILLENS TPGGKVMKTD SVENYPGFKT
IKGPDLGFHF YEQALNLGAV EAGSGIKNYK KENDVFIVEL INGKIITGLA MIIATGTKEN
LLKVPGELEY YGKGVSYCAT CDGAFYKEKD ELAVVGGGYS AIEEAIFLTR FVGKVYIIHR
RQGFRVDKKS IEKAKNNNKI EFILDSVVTE IKGSKEVESI TIKNLVDEDI RELKVSAIFP
FIGHVPNTNF INDKSILNEE GFILTNDKME TDIKGLFAAG DVRDTPFRQI ATAVSDGAIA
AQFAIKFIEN LN
//
