TRXB_SCHPO
ID TRXB_SCHPO Reviewed; 322 AA.
AC Q92375;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Thioredoxin reductase;
DE EC=1.8.1.9;
DE AltName: Full=Caffeine resistance protein 4;
GN Name=trr1; Synonyms=caf4; ORFNames=SPBC3F6.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8914513; DOI=10.1007/bf02172398;
RA Casso D., Beach D.;
RT "A mutation in a thioredoxin reductase homolog suppresses p53-induced
RT growth inhibition in the fission yeast Schizosaccharomyces pombe.";
RL Mol. Gen. Genet. 252:518-529(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9894913; DOI=10.1007/s004380050914;
RA Benko Z., Sipiczki M., Carr A.M.;
RT "Cloning of caf1+, caf2+ and caf4+ from Schizosaccharomyces pombe: their
RT involvement in multidrug resistance, UV and pH sensitivity.";
RL Mol. Gen. Genet. 260:434-443(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hong S.-M., Cho Y.-W., Lim C.-J.;
RT "Molecular characterization and regulation of a gene encoding thioredoxin
RT reductase homolog from the fission Yeast.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; THR-278 AND SER-279, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P29509};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P29509};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P29509}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29509}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; U63713; AAC49569.1; -; Genomic_DNA.
DR EMBL; AF535134; AAN01228.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA17692.1; -; Genomic_DNA.
DR PIR; T40393; T40393.
DR RefSeq; NP_001018848.1; NM_001022668.2.
DR AlphaFoldDB; Q92375; -.
DR SMR; Q92375; -.
DR BioGRID; 280434; 12.
DR STRING; 4896.SPBC3F6.03.1; -.
DR iPTMnet; Q92375; -.
DR MaxQB; Q92375; -.
DR PaxDb; Q92375; -.
DR PRIDE; Q92375; -.
DR EnsemblFungi; SPBC3F6.03.1; SPBC3F6.03.1:pep; SPBC3F6.03.
DR GeneID; 3361358; -.
DR KEGG; spo:SPBC3F6.03; -.
DR PomBase; SPBC3F6.03; trr1.
DR VEuPathDB; FungiDB:SPBC3F6.03; -.
DR eggNOG; KOG0404; Eukaryota.
DR HOGENOM; CLU_031864_5_1_1; -.
DR InParanoid; Q92375; -.
DR OMA; VDNFPGY; -.
DR PhylomeDB; Q92375; -.
DR PRO; PR:Q92375; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISS:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:PomBase.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0019430; P:removal of superoxide radicals; IC:PomBase.
DR Gene3D; 3.50.50.60; -; 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 Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Phosphoprotein; Redox-active center; Reference proteome.
FT CHAIN 1..322
FT /note="Thioredoxin reductase"
FT /id="PRO_0000166768"
FT BINDING 11..14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT BINDING 40..41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT BINDING 45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT BINDING 54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT BINDING 87
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT BINDING 145
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT BINDING 288
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT BINDING 295..297
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 278
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT DISULFID 142..145
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P29509"
SQ SEQUENCE 322 AA; 34618 MW; 3209D979DA303ECA CRC64;
MTHNKVVIIG SGPAGHTAAI YLARGELKPV MYEGMLANGI AAGGQLTTTT DVENFPGFPD
GINGTTLTEN FRAQSLRFGT EIITETVSKL DLSSRPFKYW LEGAEEEEPH TADSVILATG
ASARRLHITG EDTYWQAGIS ACAVCDGAVP IYRNKPLAVV GGGDSAAEEA QFLTKYGSKV
YVLVRRDKLR ASPIMAKRLL ANPKVEVLWN TVAEEAQGDG KLLNNLRIKN TNTNEVSDLQ
VNGLFYAIGH IPATKLVAEQ IELDEAGYIK TINGTPRTSI PGFFAAGDVQ DKVFRQAITS
AGSGCQAALL AMHYLEELED TD
