ID W7JXY5_PLAFO Unreviewed; 617 AA.
AC W7JXY5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=thioredoxin-disulfide reductase {ECO:0000256|ARBA:ARBA00012610};
DE EC=1.8.1.9 {ECO:0000256|ARBA:ARBA00012610};
GN ORFNames=CK202_4213 {ECO:0000313|EMBL:PKC45215.1}, CYL21_1047
GN {ECO:0000313|EMBL:KAF4330670.1}, PFNF54_05603
GN {ECO:0000313|EMBL:EWC85939.1};
OS Plasmodium falciparum (isolate NF54).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5843 {ECO:0000313|EMBL:EWC85939.1, ECO:0000313|Proteomes:UP000030673};
RN [1] {ECO:0000313|EMBL:EWC85939.1, ECO:0000313|Proteomes:UP000030673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF54 {ECO:0000313|EMBL:EWC85939.1,
RC ECO:0000313|Proteomes:UP000030673};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum NF54.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PKC45215.1, ECO:0000313|Proteomes:UP000232684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF54 {ECO:0000313|EMBL:PKC45215.1};
RA Bryant J.M., Baumgarten S., Scheidig-Benatar C., Scherf A.;
RT "Plasmodium falciparum NF54 genome assembly.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF4330670.1, ECO:0000313|Proteomes:UP000754359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF54 {ECO:0000313|EMBL:KAF4330670.1};
RA Baumgarten S., Treeck M., Scherf A.;
RT "Genome assembly of Plasmodium falciparum NF54 DiCre.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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DR EMBL; KE123882; EWC85939.1; -; Genomic_DNA.
DR EMBL; QFXU01000008; KAF4330670.1; -; Genomic_DNA.
DR EMBL; NYMT01000014; PKC45215.1; -; Genomic_DNA.
DR AlphaFoldDB; W7JXY5; -.
DR SMR; W7JXY5; -.
DR EnsemblProtists; EWC85939; EWC85939; PFNF54_05603.
DR VEuPathDB; PlasmoDB:PfNF54_090028900; -.
DR OMA; CFDYVKP; -.
DR Proteomes; UP000030673; Unassembled WGS sequence.
DR Proteomes; UP000232684; Unassembled WGS sequence.
DR Proteomes; UP000754359; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR NCBIfam; TIGR01438; TGR; 1.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF8; THIOREDOXIN REDUCTASE 1; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000030673}.
FT DOMAIN 118..449
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 469..594
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 617 AA; 68698 MW; 50E1692E12D73C1D CRC64;
MNNVISFIGN SSNKYFQINQ LHFIRIINKN IHSKNNLINS NSSYNVFYNK YFIKNTFQNK
NKLSSIYSKL NFSIKNMCKD KNEKKNYEHV NANEKNGYLA SEKNELTKNK VEEHTYDYDY
VVIGGGPGGM ASAKEAAAHG ARVLLFDYVK PSSQGTKWGI GGTCVNVGCV PKKLMHYAGH
MGSIFKLDSK AYGWKFDNLK HDWKKLVTTV QSHIRSLNFS YMTGLRSSKV KYINGLAKLK
DKNTVSYYLK GDLSKEETVT GKYILIATGC RPHIPDDVEG AKELSITSDD IFSLKKDPGK
TLVVGASYVA LECSGFLNSL GYDVTVAVRS IVLRGFDQQC AVKVKLYMEE QGVMFKNGIL
PKKLTKMDDK ILVEFSDKTS ELYDTVLYAI GRKGDIDGLN LESLNMNVNK SNNKIIADHL
SCTNIPSIFA VGDVAENVPE LAPVAIKAGE ILARRLFKDS DEIMDYSYIP TSIYTPIEYG
ACGYSEEKAY ELYGKSNVEV FLQEFNNLEI SAVHRQKHIR AQKDEYDLDV SSTCLAKLVC
LKNEDNRVIG FHYVGPNAGE VTQGMALALR LKVKKKDFDN CIGIHPTDAE SFMNLFVTIS
SGLSYAAKGG CGGGKCG
//
