FER_PLAF7
ID FER_PLAF7 Reviewed; 194 AA.
AC Q8IED5;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ferredoxin, apicoplast {ECO:0000303|PubMed:17251200};
DE Flags: Precursor;
GN Name=FD {ECO:0000303|PubMed:16289098};
GN ORFNames=PF3D7_1318100 {ECO:0000312|EMBL:CAD52325.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|EMBL:CAD52325.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=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., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3]
RP FUNCTION, AND INTERACTION WITH LYTB.
RX PubMed=16289098; DOI=10.1016/j.febslet.2005.10.037;
RA Roehrich R.C., Englert N., Troschke K., Reichenberg A., Hintz M.,
RA Seeber F., Balconi E., Aliverti A., Zanetti G., Koehler U., Pfeiffer M.,
RA Beck E., Jomaa H., Wiesner J.;
RT "Reconstitution of an apicoplast-localised electron transfer pathway
RT involved in the isoprenoid biosynthesis of Plasmodium falciparum.";
RL FEBS Lett. 579:6433-6438(2005).
RN [4] {ECO:0007744|PDB:1IUE}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 98-194 IN COMPLEX WITH 2FE-2S
RP IRON-SULFUR CLUSTER, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=17251200; DOI=10.1093/jb/mvm046;
RA Kimata-Ariga Y., Kurisu G., Kusunoki M., Aoki S., Sato D., Kobayashi T.,
RA Kita K., Horii T., Hase T.;
RT "Cloning and characterization of ferredoxin and ferredoxin-NADP+ reductase
RT from human malaria parasite.";
RL J. Biochem. 141:421-428(2007).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions (PubMed:16289098). By
CC transferring electrons to 4-hydroxy-3-methylbut-2-enyl diphosphate
CC reductase LytB/IspH, plays a role in the terminal step of the DOXP/MEP
CC pathway for isoprenoid precursor biosynthesis (PubMed:16289098).
CC {ECO:0000269|PubMed:16289098}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00465,
CC ECO:0000269|PubMed:17251200};
CC Note=Binds 1 2Fe-2S cluster. {ECO:0000255|PROSITE-ProRule:PRU00465,
CC ECO:0000269|PubMed:17251200};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -266 mV. {ECO:0000269|PubMed:17251200};
CC -!- INTERACTION:
CC Q8IED5; C6KT68: FNR; NbExp=3; IntAct=EBI-7046314, EBI-7046197;
CC -!- SUBCELLULAR LOCATION: Plastid, apicoplast
CC {ECO:0000305|PubMed:17251200}.
CC -!- DEVELOPMENTAL STAGE: Detected in trophozoite and schizont stages (at
CC protein level). {ECO:0000269|PubMed:17251200}.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; AL844509; CAD52325.1; -; Genomic_DNA.
DR RefSeq; XP_001349917.1; XM_001349881.1.
DR PDB; 1IUE; X-ray; 1.70 A; A/B=98-194.
DR PDBsum; 1IUE; -.
DR AlphaFoldDB; Q8IED5; -.
DR SMR; Q8IED5; -.
DR IntAct; Q8IED5; 2.
DR MINT; Q8IED5; -.
DR STRING; 5833.MAL13P1.95; -.
DR EnsemblProtists; CAD52325; CAD52325; PF3D7_1318100.
DR GeneID; 813986; -.
DR KEGG; pfa:PF3D7_1318100; -.
DR VEuPathDB; PlasmoDB:PF3D7_1318100; -.
DR HOGENOM; CLU_082632_1_2_1; -.
DR InParanoid; Q8IED5; -.
DR OMA; PLNYMYG; -.
DR PhylomeDB; Q8IED5; -.
DR EvolutionaryTrace; Q8IED5; -.
DR Proteomes; UP000001450; Chromosome 13.
DR GO; GO:0020011; C:apicoplast; IDA:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; ISS:GeneDB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR010241; Fd_pln.
DR Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR02008; fdx_plant; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Apicoplast; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Plastid; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..19
FT /note="Apicoplast"
FT /evidence="ECO:0000255"
FT CHAIN 20..194
FT /note="Ferredoxin, apicoplast"
FT /id="PRO_5004311090"
FT DOMAIN 99..189
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 135
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:17251200, ECO:0007744|PDB:1IUE"
FT BINDING 140
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:17251200, ECO:0007744|PDB:1IUE"
FT BINDING 143
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:17251200, ECO:0007744|PDB:1IUE"
FT BINDING 173
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:17251200, ECO:0007744|PDB:1IUE"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:1IUE"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:1IUE"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:1IUE"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:1IUE"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:1IUE"
FT HELIX 162..166
FT /evidence="ECO:0007829|PDB:1IUE"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1IUE"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1IUE"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1IUE"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:1IUE"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:1IUE"
SQ SEQUENCE 194 AA; 22721 MW; ACE738196F816D3E CRC64;
MNIVILLLIL TFSIKHSNTY KLKNTYIPIN YMYHNNKNIL RSQKSKLFLN FLSNNQLANS
NKQTCFFKSN IKSSISNIDN YDYIRKRYIN TSNKNKLFYN ITLRTNDGEK KIECNEDEYI
LDASERQNVE LPYSCRGGSC STCAAKLVEG EVDNDDQSYL DEEQIKKKYI LLCTCYPKSD
CVIETHKEDE LHDM
