FRO1_ARATH
ID FRO1_ARATH Reviewed; 704 AA.
AC Q9LMM2; P92950;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable ferric reduction oxidase 1;
DE Short=AtFRO1;
DE EC=1.16.1.7;
DE AltName: Full=Ferric-chelate reductase 1;
GN Name=FRO1; OrderedLocusNames=At1g01590; ORFNames=F22L4.13;
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10067892; DOI=10.1038/17800;
RA Robinson N.J., Procter C.M., Connolly E.L., Guerinot M.L.;
RT "A ferric-chelate reductase for iron uptake from soils.";
RL Nature 397:694-697(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Ferric chelate reductase involved in iron reduction in roots
CC (By similarity). May participate in the transport of electrons to a
CC Fe(3+) ion via FAD and heme intermediates. {ECO:0000250}.
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: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques. Detected in roots.
CC {ECO:0000269|PubMed:10067892, ECO:0000269|PubMed:16362328}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
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DR EMBL; Y09581; CAA70769.1; -; Genomic_DNA.
DR EMBL; AC061957; AAF81317.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27309.1; -; Genomic_DNA.
DR PIR; F86146; F86146.
DR RefSeq; NP_171665.1; NM_100041.2.
DR AlphaFoldDB; Q9LMM2; -.
DR SMR; Q9LMM2; -.
DR STRING; 3702.AT1G01590.1; -.
DR PaxDb; Q9LMM2; -.
DR PRIDE; Q9LMM2; -.
DR ProteomicsDB; 230548; -.
DR EnsemblPlants; AT1G01590.1; AT1G01590.1; AT1G01590.
DR GeneID; 837194; -.
DR Gramene; AT1G01590.1; AT1G01590.1; AT1G01590.
DR KEGG; ath:AT1G01590; -.
DR Araport; AT1G01590; -.
DR TAIR; locus:2025366; AT1G01590.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_014777_1_0_1; -.
DR InParanoid; Q9LMM2; -.
DR OMA; KMTLICA; -.
DR OrthoDB; 190356at2759; -.
DR PhylomeDB; Q9LMM2; -.
DR BioCyc; ARA:AT1G01590-MON; -.
DR PRO; PR:Q9LMM2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMM2; 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; IMP: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; 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 SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Electron transport; FAD; Flavoprotein; Heme; Ion transport; Iron; Membrane;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..704
FT /note="Probable ferric reduction oxidase 1"
FT /id="PRO_0000413199"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..36
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 37..62
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..81
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 82..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..139
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 140..207
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..231
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 232..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..307
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 308..329
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 351..550
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..573
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 574..592
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 593..614
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 615..704
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 174..294
FT /note="Ferric oxidoreductase"
FT DOMAIN 323..430
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
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:0000305"
FT BINDING 223
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:0000305"
FT BINDING 284
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:0000305"
FT BINDING 297
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:0000305"
FT BINDING 372..375
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 422..425
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT CONFLICT 443
FT /note="G -> A (in Ref. 1; CAA70769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 704 AA; 79600 MW; DB027A91FD282DD9 CRC64;
MGVGEMNKEV IDKVIKFLMM VILMGTIVIW IMMPTSTYKE IWLTSMRAKL GKSIYYGRPG
VNLLVYMFPM ILLAFLGCIY LHLKKSTTVN QFNSGVEKKR AKFGALRRPM LVNGPLGIVT
VTEVMFLTMF MALLLWSLAN YMYRTFVNVT SESAATDGNN LWQARLDLIA VRIGIVGNIC
LAFLFYPVAR GSSLLAAVGL TSESSIKYHI WLGHLVMIIF TSHGLCYFIY WISKNQLVSK
MLEWDRTAVS NLAGEIALVA GLMMWVTTYP KIRRRLFEVF FYSHYLYIVF MLFFVFHVGI
SHALIPLPGF YIFLVDRFLR FLQSRNNVKL VSARVLPCDT VELNFSKNPM LMYSPTSTMF
VNIPSISKLQ WHPFTIISSS KLEPETLSVM IKSQGKWSTK LYDMLSSSSS DQINRLAVSV
EGPYGPSSTD FLRHESLVMV SGGSGITPFI SIVRDLFYMS STHKCKIPKM TLICAFKNSS
DLSMLDLILP TSGLTTDMAS FVDIQIKAFV TREEKTSVKE STHNRNIIKT RHFKPNVSDQ
PISPILGPNS WLCLAAILSS SFMIFIVIIA IITRYHIHPI DQNSEKYTWA YKSLIYLVSI
SITVVTTSTA AMLWNKKKYY AKNDQYVDNL SPVIIESSPQ QLISQSTDIH YGERPNLNKL
LVGLKGSSVG ILVCGPKKMR QKVAKICSFG SAENLHFESI SFSW
