ID Q46JS9_PROMT Unreviewed; 458 AA.
AC Q46JS9;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN OrderedLocusNames=PMN2A_0758 {ECO:0000313|EMBL:AAZ58249.1};
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59920 {ECO:0000313|EMBL:AAZ58249.1, ECO:0000313|Proteomes:UP000002535};
RN [1] {ECO:0000313|EMBL:AAZ58249.1, ECO:0000313|Proteomes:UP000002535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A {ECO:0000313|EMBL:AAZ58249.1,
RC ECO:0000313|Proteomes:UP000002535};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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:RU003881};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003881};
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; CP000095; AAZ58249.1; -; Genomic_DNA.
DR RefSeq; WP_011294846.1; NC_007335.2.
DR AlphaFoldDB; Q46JS9; -.
DR STRING; 59920.PMN2A_0758; -.
DR KEGG; pmn:PMN2A_0758; -.
DR HOGENOM; CLU_031864_5_4_3; -.
DR OrthoDB; 9806179at2; -.
DR PhylomeDB; Q46JS9; -.
DR Proteomes; UP000002535; 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 Gene3D; 3.40.30.10; Glutaredoxin; 1.
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 InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01292; TRX_reduct; 1.
DR PANTHER; PTHR48105:SF26; NADPH-DEPENDENT THIOREDOXIN REDUCTASE 3; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_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:UP000002535}.
FT DOMAIN 340..458
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 458 AA; 50216 MW; 5A3000ABA3F71FF9 CRC64;
MPAENKELKT ENLVIIGSGP AGYTAAIYAA RANLQPLIIT GFEKGGIPGG QLMTTTFVEN
FPGFPNGVQG PELMDLIKAQ AVRWGTNLIE EDAISIDLSK RPFSIVTTTQ KIKTNSLIIS
TGASANRLGL KNEKLFWSKG ISACAICDGA TPQFRDEELA VVGGGDSACE EAEYLTKYGS
HVHLLVRSRK LRASAAMADR VEANPNITIH WETELLDVLG NDWLEKLKVK RRDTNQEEEI
LAKGLFYAIG HTPNTSLFTN QLSTDSKGYL LTQPGRPETS LEGVYAAGDV ADSEWRQGVT
AAGSGCKAAL AAERWLTKNN LATLIKRVEL EPSKADTTKI LEVSNEANFD PEKTWQKGSY
ALRKLYHETE KPLFVVYTSS SCGPCHILKP QLHRVLNESK GKAIGVEIDI ENDQDIAKQA
EVSGTPTVHL FKNKELKKQW KGVKTRSEYK AALDELIN
//
