ID A0A094BBF8_9PEZI Unreviewed; 702 AA.
AC A0A094BBF8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003881};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003881};
GN ORFNames=V492_06947 {ECO:0000313|EMBL:KFY07662.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY07662.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY07662.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY07662.1,
RC ECO:0000313|Proteomes:UP000029299};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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|RuleBase:RU003881};
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 -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333}.
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:KFY07662.1}.
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DR EMBL; JPJU01002505; KFY07662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094BBF8; -.
DR STRING; 1420902.A0A094BBF8; -.
DR HOGENOM; CLU_015538_0_0_1; -.
DR Proteomes; UP000029299; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
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:RU003881};
KW Flavoprotein {ECO:0000256|RuleBase:RU003881};
KW NADP {ECO:0000256|RuleBase:RU003881};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003881};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003881};
KW Reference proteome {ECO:0000313|Proteomes:UP000029299};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..702
FT /note="Thioredoxin reductase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001897775"
FT DOMAIN 356..656
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT REGION 114..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 74169 MW; A1D4453069DA1DF8 CRC64;
MISPLSSISL SLLVLAITVQ ATSIISLGGN FQLLPFGITG ECRTVYNQPI EGCSARDFQA
GSACSQACVA SLNNISNTLN VVCPGVIVDS RTLLGRIFRN MLIESVCNAV EAPSQSSAPA
DNATTPPSTP VATTQAPSQS TTAEAPTTTS EKAKSSAVLG IGDPEPTSES TSEPTPEPTA
GATTSEIQAP QSTTANKQAK PSERSRLQEQ IDANRFSGGG SPFDNIVSEN GAPHRRSNAG
FCQTAFENSM DSSSKLLPPR ALLYTSSITK WPPKLTSTPP KTLHSDPPRD LDTSPNPASN
LTHEKSAKLF SSAFGRSTTL LKSSSGLPLV AAASLTRQKS TAPAPVIASS RMMHSKVVII
GSGPAAHTAA IYLARAELKP VLYEGMMANG IAAGGQLTTT TDVENFPGFP NGIGGMALME
DMRKQSERFG TEVVSETVAK VDLSSRPFKY WLEYAEDAAP HTADALIIAT GASARRLDLP
GEQKYWQNGI SACAVCDGAV PIFRNKPLVV IGGGDSAAEE ALFLTKYGSH VTVLVRKDHL
RASKTMAKRL LTNKKVTVRF NSVGGEVTGD DRGLMSHMIV KNVLTGEEEN MEANGLFYAV
GHDPATALIK GQLETDSEGY LVTKPGTSYT NKVGVFAAGD VQDKRYRQAI TSAGSGCIAA
LEAEKYLSEL EDGEHLPLEE EEKNAKKGVA EDAPEYRTNP LL
//
