FRDA_ARATH
ID FRDA_ARATH Reviewed; 187 AA.
AC Q9ZR07; Q6GKV0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Frataxin, mitochondrial;
DE Short=Fxn;
DE EC=1.16.3.1;
DE Flags: Precursor;
GN Name=FH; OrderedLocusNames=At4g03240; ORFNames=F4C21.17;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15474026; DOI=10.1016/j.febslet.2004.09.003;
RA Busi M.V., Zabaleta E.J., Araya A., Gomez-Casati D.F.;
RT "Functional and molecular characterization of the frataxin homolog from
RT Arabidopsis thaliana.";
RL FEBS Lett. 576:141-144(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17092311; DOI=10.1111/j.1365-313x.2006.02923.x;
RA Busi M.V., Maliandi M.V., Valdez H., Clemente M., Zabaleta E.J., Araya A.,
RA Gomez-Casati D.F.;
RT "Deficiency of Arabidopsis thaliana frataxin alters activity of
RT mitochondrial Fe-S proteins and induces oxidative stress.";
RL Plant J. 48:873-882(2006).
RN [7]
RP FUNCTION, AND INTERACTION WITH NIFS1.
RX PubMed=22511606; DOI=10.1093/mp/sss037;
RA Turowski V.R., Busi M.V., Gomez-Casati D.F.;
RT "Structural and functional studies of the mitochondrial cysteine
RT desulfurase from Arabidopsis thaliana.";
RL Mol. Plant 5:1001-1010(2012).
CC -!- FUNCTION: Promotes the biosynthesis of heme as well as the assembly and
CC repair of iron-sulfur clusters by delivering Fe(2+) to proteins
CC involved in these pathways (PubMed:17092311). May play a role in the
CC protection against iron-catalyzed oxidative stress through its ability
CC to catalyze the oxidation of Fe(2+) to Fe(3+) (PubMed:17092311). May be
CC able to store large amounts of the metal in the form of a ferrihydrite
CC mineral by oligomerization (PubMed:17092311). Binds to the
CC mitochondrial cysteine desulfurase NIFS1 and increases its activity
CC (PubMed:22511606). {ECO:0000269|PubMed:17092311,
CC ECO:0000269|PubMed:22511606}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC -!- SUBUNIT: Monomer. Oligomer (By similarity). Interacts with NIFS1
CC (PubMed:22511606). {ECO:0000250, ECO:0000269|PubMed:22511606}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17092311}.
CC -!- SIMILARITY: Belongs to the frataxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD14452.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB77809.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY649366; AAU11485.1; -; mRNA.
DR EMBL; AC005275; AAD14452.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161496; CAB77809.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82296.1; -; Genomic_DNA.
DR EMBL; BT014964; AAT47815.1; -; mRNA.
DR EMBL; AK176448; BAD44211.1; -; mRNA.
DR EMBL; AK176831; BAD44594.1; -; mRNA.
DR PIR; B85041; B85041.
DR RefSeq; NP_192233.2; NM_116562.4.
DR AlphaFoldDB; Q9ZR07; -.
DR SMR; Q9ZR07; -.
DR BioGRID; 13304; 1.
DR STRING; 3702.AT4G03240.1; -.
DR PaxDb; Q9ZR07; -.
DR PRIDE; Q9ZR07; -.
DR ProteomicsDB; 230528; -.
DR EnsemblPlants; AT4G03240.1; AT4G03240.1; AT4G03240.
DR GeneID; 828013; -.
DR Gramene; AT4G03240.1; AT4G03240.1; AT4G03240.
DR KEGG; ath:AT4G03240; -.
DR Araport; AT4G03240; -.
DR TAIR; locus:2125477; AT4G03240.
DR eggNOG; KOG3413; Eukaryota.
DR HOGENOM; CLU_080880_2_0_1; -.
DR InParanoid; Q9ZR07; -.
DR OMA; QGWIYRR; -.
DR OrthoDB; 1372185at2759; -.
DR PhylomeDB; Q9ZR07; -.
DR BioCyc; ARA:AT4G03240-MON; -.
DR BRENDA; 4.99.1.1; 399.
DR SABIO-RK; Q9ZR07; -.
DR PRO; PR:Q9ZR07; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZR07; baseline and differential.
DR Genevisible; Q9ZR07; AT.
DR GO; GO:0009507; C:chloroplast; IDA:CACAO.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:CACAO.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0004322; F:ferroxidase activity; IBA:GO_Central.
DR GO; GO:0034986; F:iron chaperone activity; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IMP:TAIR.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0018283; P:iron incorporation into metallo-sulfur cluster; IBA:GO_Central.
DR GO; GO:1903329; P:regulation of iron-sulfur cluster assembly; IMP:TAIR.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR Gene3D; 3.30.920.10; -; 1.
DR InterPro; IPR017789; Frataxin.
DR InterPro; IPR002908; Frataxin/CyaY.
DR InterPro; IPR036524; Frataxin/CyaY_sf.
DR InterPro; IPR020895; Frataxin_CS.
DR PANTHER; PTHR16821; PTHR16821; 1.
DR Pfam; PF01491; Frataxin_Cyay; 1.
DR SMART; SM01219; Frataxin_Cyay; 1.
DR SUPFAM; SSF55387; SSF55387; 1.
DR TIGRFAMs; TIGR03421; FeS_CyaY; 1.
DR TIGRFAMs; TIGR03422; mito_frataxin; 1.
DR PROSITE; PS01344; FRATAXIN_1; 1.
DR PROSITE; PS50810; FRATAXIN_2; 1.
PE 1: Evidence at protein level;
KW Heme biosynthesis; Ion transport; Iron; Iron storage; Iron transport;
KW Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..187
FT /note="Frataxin, mitochondrial"
FT /id="PRO_0000193926"
SQ SEQUENCE 187 AA; 21430 MW; FAFA6A8AF7FD7534 CRC64;
MATASRFLLR KLPRFLKLSP TLLRSNGVRV SSNLIQDSIE PLDSFWRIGS RIRHDSLTTR
SFSSQGPASV DYSSVLQEEE FHKLANFTIN HLLEKIEDYG DNVQIDGFDI DYGNEVLTLK
LGSLGTYVLN KQTPNRQIWM SSPVSGPSRF DWDRDANAWI YRRTEAKLHK LLEEELENLC
GEPIQLS
