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Database: UniProt
Entry: Q7KQL8
LinkDB: Q7KQL8
Original site: Q7KQL8 
ID   THIO_PLAF7              Reviewed;         104 AA.
AC   Q7KQL8;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-APR-2013, entry version 67.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   ORFNames=PF14_0545;
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7;
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T.,
RA   James K.D., Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A.,
RA   Kyes S., Chan M.-S., Nene V., Shallom S.J., Suh B., Peterson J.,
RA   Angiuoli S., Pertea M., Allen J., Selengut J., Haft D., Mather M.W.,
RA   Vaidya A.B., Martin D.M.A., Fairlamb A.H., Fraunholz M.J., Roos D.S.,
RA   Ralph S.A., McFadden G.I., Cummings L.M., Subramanian G.M.,
RA   Mungall C., Venter J.C., Carucci D.J., Hoffman S.L., Newbold C.,
RA   Davis R.W., Fraser C.M., Barrell B.G.;
RT   "Genome sequence of the human malaria parasite Plasmodium
RT   falciparum.";
RL   Nature 419:498-511(2002).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS), AND DISULFIDE BOND.
RA   Robien M.A., Hol W.G.J.;
RT   "Structural genomics of pathogenic protozoa initial structural
RT   analysis of Plasmodium falciparum thioredoxin.";
RL   Submitted (APR-2004) to the PDB data bank.
CC   -!- FUNCTION: Participates in various redox reactions through the
CC       reversible oxidation of its active center dithiol to a disulfide
CC       and catalyzes dithiol-disulfide exchange reactions (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; AE014187; AAN37158.1; -; Genomic_DNA.
DR   RefSeq; XP_001348719.1; XM_001348683.1.
DR   PDB; 1SYR; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L=1-104.
DR   PDBsum; 1SYR; -.
DR   ProteinModelPortal; Q7KQL8; -.
DR   SMR; Q7KQL8; 1-103.
DR   IntAct; Q7KQL8; 1.
DR   MINT; MINT-1625012; -.
DR   STRING; 5833.PF14_0545-1; -.
DR   EnsemblProtists; PF14_0545:mRNA; PF14_0545:pep; PF14_0545.
DR   GeneID; 812127; -.
DR   KEGG; pfa:PF14_0545; -.
DR   EuPathDB; PlasmoDB:PF3D7_1457200; -.
DR   HOGENOM; HOG000292977; -.
DR   KO; K03671; -.
DR   OMA; LLNWISN; -.
DR   ProtClustDB; PTZ00051; -.
DR   EvolutionaryTrace; Q7KQL8; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.30.10; -; 1.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10438; PTHR10438; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; Thioredoxin; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
DR   TIGRFAMs; TIGR01068; thioredoxin; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Disulfide bond; Electron transport;
KW   Redox-active center; Reference proteome; Transport.
FT   CHAIN         1    104       Thioredoxin.
FT                                /FTId=PRO_0000233976.
FT   DOMAIN        2    104       Thioredoxin.
FT   ACT_SITE     30     30       Nucleophile (By similarity).
FT   ACT_SITE     33     33       Nucleophile (By similarity).
FT   SITE         24     24       Deprotonates C-terminal active site Cys
FT                                (By similarity).
FT   SITE         31     31       Contributes to redox potential value (By
FT                                similarity).
FT   SITE         32     32       Contributes to redox potential value (By
FT                                similarity).
FT   DISULFID     30     33       Redox-active.
FT   STRAND        3      5
FT   HELIX         8     17
FT   STRAND       19     26
FT   HELIX        31     46
FT   STRAND       50     56
FT   TURN         57     60
FT   HELIX        61     66
FT   STRAND       71     79
FT   STRAND       82     89
FT   HELIX        92    100
SQ   SEQUENCE   104 AA;  11716 MW;  0129998AEB88770C CRC64;
     MVKIVTSQAE FDSIISQNEL VIVDFFAEWC GPCKRIAPFY EECSKTYTKM VFIKVDVDEV
     SEVTEKENIT SMPTFKVYKN GSSVDTLLGA NDSALKQLIE KYAA
//
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