FRO8_ARATH
ID FRO8_ARATH Reviewed; 728 AA.
AC Q8VY13; Q9FGS9;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Ferric reduction oxidase 8, mitochondrial;
DE Short=AtFRO8;
DE EC=1.16.1.7;
DE AltName: Full=Ferric-chelate reductase 8;
DE Flags: Precursor;
GN Name=FRO8; OrderedLocusNames=At5g50160; ORFNames=K6A12.2;
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], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY
RP IRON.
RX PubMed=16006655; DOI=10.1093/pcp/pci163;
RA Wu H., Li L., Du J., Yuan Y., Cheng X., Ling H.Q.;
RT "Molecular and biochemical characterization of the Fe(III) chelate
RT reductase gene family in Arabidopsis thaliana.";
RL Plant Cell Physiol. 46:1505-1514(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION BY IRON AND COPPER.
RX PubMed=16362328; DOI=10.1007/s00425-005-0165-0;
RA Mukherjee I., Campbell N.H., Ash J.S., Connolly E.L.;
RT "Expression profiling of the Arabidopsis ferric chelate reductase (FRO)
RT gene family reveals differential regulation by iron and copper.";
RL Planta 223:1178-1190(2006).
RN [7]
RP GENE FAMILY, NOMENCLATURE, AND SUBCELLULAR LOCATION.
RX DOI=10.1016/j.plantsci.2009.02.011;
RA Jeong J., Connolly E.L.;
RT "Iron uptake mechanisms in plants: Functions of the FRO family of ferric
RT reductases.";
RL Plant Sci. 176:709-714(2009).
CC -!- FUNCTION: Ferric chelate reductase probably involved in iron reduction
CC in leaf veins for transport. May participate in the transport of
CC electrons to a Fe(3+) ion via FAD and heme intermediates.
CC {ECO:0000269|PubMed:16006655}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-
CC siderophore + NADH; Xref=Rhea:RHEA:15061, Rhea:RHEA-COMP:11342,
CC Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.16.1.7;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in shoots. Detected in roots, pedicels,
CC flowers, siliques and leaf veins. {ECO:0000269|PubMed:16006655,
CC ECO:0000269|PubMed:16362328}.
CC -!- INDUCTION: Down-regulated in shoots by copper deficiency. Not regulated
CC by iron availability. {ECO:0000269|PubMed:16006655,
CC ECO:0000269|PubMed:16362328}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09387.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB024031; BAB09387.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95905.1; -; Genomic_DNA.
DR EMBL; AY074287; AAL66984.1; -; mRNA.
DR EMBL; BT003007; AAO22815.1; -; mRNA.
DR RefSeq; NP_199827.2; NM_124395.5.
DR AlphaFoldDB; Q8VY13; -.
DR SMR; Q8VY13; -.
DR STRING; 3702.AT5G50160.1; -.
DR TCDB; 5.B.1.4.1; the phagocyte (gp91(phox)) nadph oxidase family.
DR PaxDb; Q8VY13; -.
DR PRIDE; Q8VY13; -.
DR ProteomicsDB; 230563; -.
DR EnsemblPlants; AT5G50160.1; AT5G50160.1; AT5G50160.
DR GeneID; 835081; -.
DR Gramene; AT5G50160.1; AT5G50160.1; AT5G50160.
DR KEGG; ath:AT5G50160; -.
DR Araport; AT5G50160; -.
DR TAIR; locus:2157697; AT5G50160.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_014777_1_0_1; -.
DR InParanoid; Q8VY13; -.
DR OMA; TGDRHFY; -.
DR OrthoDB; 190356at2759; -.
DR PhylomeDB; Q8VY13; -.
DR BioCyc; ARA:AT5G50160-MON; -.
DR PRO; PR:Q8VY13; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VY13; baseline and differential.
DR Genevisible; Q8VY13; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0140618; F:ferric-chelate reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.80; -; 2.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00466; GP91PHOX.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Electron transport; FAD; Flavoprotein; Heme; Ion transport; Iron; Membrane;
KW Metal-binding; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 25..728
FT /note="Ferric reduction oxidase 8, mitochondrial"
FT /id="PRO_0000413206"
FT TRANSMEM 56..74
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 104..127
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 194..217
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 269..293
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 537..559
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 595..616
FT /note="Helical"
FT /evidence="ECO:0000250"
FT DOMAIN 159..281
FT /note="Ferric oxidoreductase"
FT DOMAIN 300..418
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 195
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 358..361
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 410..413
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 728 AA; 83230 MW; A1E5BFD18FB1D2B0 CRC64;
MAKVLTLLVL RLLMNLLLIG WISLWIIKPT TIWIQSWRQA EDTARHTFFG YYGLNFAVFS
FPPIALSIVG LIYLSLLPQH HHPTRGGRGA AITVSRPAII NSFIGIVSCF EILALLLFLL
FLAWNFYARV SNDFKKLMPV KTMNLNLWQL KYYRVATRFG LLAEACLSLL LFPVLRGLSM
FRLLNIEFAA SVKYHVWFGT GLIFFSLVHG GSTLFIWTIT HHIEEEIWKW QRTGRVYVAG
LISLVTGLLM WITSLPQIRR KNFEVFYYTH HLYIVFLVAF LFHAGDRHFY WVLPGMFLFG
LDKILRIVQS RSESCILSAN LFSCKAIELV LPKDPMLNYA PSSFIFLNIP LVSRFQWHPF
SIISSSSVDK HSLSIMMKCE GDWTNSVYNK IEEAANCENK INNIIVRVEG PYGPASVDFL
RYDNLFLVAG GIGITPFLSI LKELASKNRL KSPKRVQLVF AVRTFQDLNM LLPIASIIFN
PIYNLNLKLK VFVTQEKKPS NGTTTLQEFL AQSQVQSIHL GTDEDYSRFP IRGPESFRWL
ATLVLITVLT FLGFLIGLSH FFIPSEHKNH SGVMKLAASG AMKTAKEKVP SWVPDLIIIV
SYVIAISVGG FAATILQRRR KHKEAPRMSK EVVIKPEERN FTELKPIPIT EEHEIHIGER
PKLEEIMSEF EKNLRGWSSV GVLVCGPESV KEAVASMCRQ WPQCFGVEDL RRSRMKMNLN
FHSLNFNL
