FRO5_ARATH
ID FRO5_ARATH Reviewed; 707 AA.
AC Q9FLW2; F4KFN9;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Ferric reduction oxidase 5;
DE Short=AtFRO5;
DE EC=1.16.1.7;
DE AltName: Full=Ferric-chelate reductase 5;
GN Name=FRO5; OrderedLocusNames=At5g23990; ORFNames=MZF18.13;
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, AND TISSUE SPECIFICITY.
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 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 [5]
RP GENE FAMILY, AND NOMENCLATURE.
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).
RN [6]
RP FUNCTION, AND INDUCTION BY COPPER DEFICIENCY.
RX PubMed=22374396; DOI=10.1105/tpc.111.090431;
RA Bernal M., Casero D., Singh V., Wilson G.T., Grande A., Yang H.,
RA Dodani S.C., Pellegrini M., Huijser P., Connolly E.L., Merchant S.S.,
RA Kraemer U.;
RT "Transcriptome sequencing identifies SPL7-regulated copper acquisition
RT genes FRO4/FRO5 and the copper dependence of iron homeostasis in
RT Arabidopsis.";
RL Plant Cell 24:738-761(2012).
CC -!- FUNCTION: Ferric chelate reductase probably involved in iron reduction
CC in shoots. May participate in the transport of electrons to a Fe(3+)
CC ion via FAD and heme intermediates. May act in iron metabolism in
CC reproductive organs (PubMed:16006655). May function as root surface
CC cupric chelate reductase and participate in the reduction of Cu(2+),
CC for Cu(+) acquisition via Cu(+) transporters in response to copper
CC deficiency (PubMed:22374396). {ECO:0000269|PubMed:16006655,
CC ECO:0000269|PubMed:22374396}.
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: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FLW2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FLW2-2; Sequence=VSP_041874;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, shoots, pedicels
CC and inflorescence stems, flowers, sepals, stigmas and anther filaments.
CC {ECO:0000269|PubMed:16006655, ECO:0000269|PubMed:16362328}.
CC -!- INDUCTION: Up-regulated in roots and shoots by iron deficiency and
CC copper deficiency (PubMed:16362328). Induced by copper deficiency in a
CC SPL7-dependent manner (PubMed:22374396). {ECO:0000269|PubMed:16362328,
CC ECO:0000269|PubMed:22374396}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
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DR EMBL; AB009056; BAB08722.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93243.1; -; Genomic_DNA.
DR RefSeq; NP_197787.1; NM_122304.1. [Q9FLW2-2]
DR AlphaFoldDB; Q9FLW2; -.
DR SMR; Q9FLW2; -.
DR BioGRID; 17739; 2.
DR PRIDE; Q9FLW2; -.
DR ProteomicsDB; 230045; -. [Q9FLW2-1]
DR EnsemblPlants; AT5G23990.1; AT5G23990.1; AT5G23990. [Q9FLW2-2]
DR GeneID; 832464; -.
DR Gramene; AT5G23990.1; AT5G23990.1; AT5G23990. [Q9FLW2-2]
DR KEGG; ath:AT5G23990; -.
DR Araport; AT5G23990; -.
DR TAIR; locus:2178687; AT5G23990.
DR InParanoid; Q9FLW2; -.
DR PhylomeDB; Q9FLW2; -.
DR BioCyc; ARA:AT5G23990-MON; -.
DR BRENDA; 1.16.1.10; 399.
DR PRO; PR:Q9FLW2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLW2; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Electron transport; FAD; Flavoprotein;
KW Heme; Ion transport; Iron; Membrane; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..707
FT /note="Ferric reduction oxidase 5"
FT /id="PRO_0000413203"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..29
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 30..54
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..73
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 74..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..130
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 131..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..222
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 223..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..297
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 298..319
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 341..533
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..556
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 557..576
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..598
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 599..707
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 165..284
FT /note="Ferric oxidoreductase"
FT DOMAIN 313..416
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 608..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 200
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:0000255"
FT BINDING 214
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:0000255"
FT BINDING 274
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:0000255"
FT BINDING 287
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:0000255"
FT BINDING 362..365
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 408..411
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT VAR_SEQ 42..154
FT /note="YLKTTYFGPQGMNLVLLTVPMMFIAVLSCVYLHTQKQPSQTQSLYKCREWKV
FT KGRMGRVMMVMNPLGIVTATELTFSLLFLALLVWALSNYLYLSYHVHLHNHDNANDMCR
FT WQ -> HESCATHGSNDVHCGSELCLFAYPKATLPNSKRMEGKRENGEGDDGYEPIGDS
FT DSHRVDFFSV (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041874"
SQ SEQUENCE 707 AA; 81166 MW; E231558EEE935993 CRC64;
MGNMRSLVKM LMVVLFLGWI FVWIMISTNR FQNIWTPKLA KYLKTTYFGP QGMNLVLLTV
PMMFIAVLSC VYLHTQKQPS QTQSLYKCRE WKVKGRMGRV MMVMNPLGIV TATELTFSLL
FLALLVWALS NYLYLSYHVH LHNHDNANDM CRWQAKFRAF GLRIGYVGHY CWAFLFFPVT
RASTILPLVG LTSESSIKYH IWLGHVSNFC FLVHTVVFLI YWAMVNKLME TFAWNATYVP
NLAGTIAMVI GIAIWVTSLP SFRRKKFEIF FYTHHLYGLY IVFYAIHVGD SWFCMILPNI
FLFFIDRYLR FLQSTKRSRL VSAKILPSDN LELTFAKTSG LHYTPTSILF LHVPSISKLQ
WHPFTITSSS NLEKDTLSVV IRKQGSWTQK LYTHLSSSID SLEVSTEGPY GPNSFDVSRH
DSLILVGGGS GVTPFISVIR ELIFQSQNRS TKLPNVLLVC AFKNYHDLAF LDLIFPSDIS
VSDISKLNLR IEAYITREDK KPETTDDHKL LQTKWFKPQP LDSPISPVLG PNNFLWLGVV
ILSSFVMFLL LIGIVTRYYI YPVDHNTGSI YNFTYRVLWV MFLGCVCIFI SSSIIFLWRK
KENKEGDKDS KKQVQSVEFQ TPTSSPGSWF HGHERELESV PYQSIVQATS VHFGSKPNLK
KILFEAEGSE DVGVMVCGPK KMRHEVAKIC SSGLAKNLHF EAISFNW
