FRO6_ARATH
ID FRO6_ARATH Reviewed; 738 AA.
AC Q8RWS6; Q0WLX7; Q9LTA0;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Ferric reduction oxidase 6;
DE Short=AtFRO6;
DE EC=1.16.1.7;
DE AltName: Full=Ferric-chelate reductase 6;
GN Name=FRO6; OrderedLocusNames=At5g49730; ORFNames=K2I5.9;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 260-738.
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 INDUCTION BY LIGHT AND IRON, AND DEVELOPMENTAL STAGE.
RX PubMed=16489134; DOI=10.1104/pp.105.074138;
RA Feng H., An F., Zhang S., Ji Z., Ling H.Q., Zuo J.;
RT "Light-regulated, tissue-specific, and cell differentiation-specific
RT expression of the Arabidopsis Fe(III)-chelate reductase gene AtFRO6.";
RL Plant Physiol. 140:1345-1354(2006).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18647837; DOI=10.1073/pnas.0708367105;
RA Jeong J., Cohu C., Kerkeb L., Pilon M., Connolly E.L., Guerinot M.L.;
RT "Chloroplast Fe(III) chelate reductase activity is essential for seedling
RT viability under iron limiting conditions.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10619-10624(2008).
RN [9]
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 [10]
RP FUNCTION.
RX PubMed=21104018; DOI=10.1007/s11033-010-0472-9;
RA Li L.Y., Cai Q.Y., Yu D.S., Guo C.H.;
RT "Overexpression of AtFRO6 in transgenic tobacco enhances ferric chelate
RT reductase activity in leaves and increases tolerance to iron-deficiency
RT chlorosis.";
RL Mol. Biol. Rep. 38:3605-3613(2011).
CC -!- FUNCTION: Ferric chelate reductase involved in iron uptake by shoot and
CC leaf cells. May participate in the transport of electrons to a Fe(3+)
CC ion via FAD and heme intermediates. {ECO:0000269|PubMed:16006655,
CC ECO:0000269|PubMed:18647837, ECO:0000269|PubMed:21104018}.
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 -!- TISSUE SPECIFICITY: Expressed in shoots and leaves. Detected in
CC cotyledons, stems, siliques, flowers, sepals, anther filaments and
CC stigmas, but not in roots. {ECO:0000269|PubMed:16006655,
CC ECO:0000269|PubMed:16362328}.
CC -!- DEVELOPMENTAL STAGE: Not expressed in germinating seeds. Expressed
CC during cell or organ differentiation. {ECO:0000269|PubMed:16489134}.
CC -!- INDUCTION: Down-regulated in shoots by copper deficiency. Not regulated
CC by iron availability. Light dependent expression.
CC {ECO:0000269|PubMed:16362328, ECO:0000269|PubMed:16489134}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA98161.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB025613; BAA98161.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95851.1; -; Genomic_DNA.
DR EMBL; AY091140; AAM14089.1; -; mRNA.
DR EMBL; AY114002; AAM45050.1; -; mRNA.
DR EMBL; AK230058; BAF01880.1; -; mRNA.
DR RefSeq; NP_199784.2; NM_124351.4.
DR AlphaFoldDB; Q8RWS6; -.
DR SMR; Q8RWS6; -.
DR STRING; 3702.AT5G49730.1; -.
DR PaxDb; Q8RWS6; -.
DR PRIDE; Q8RWS6; -.
DR ProteomicsDB; 230562; -.
DR EnsemblPlants; AT5G49730.1; AT5G49730.1; AT5G49730.
DR GeneID; 835036; -.
DR Gramene; AT5G49730.1; AT5G49730.1; AT5G49730.
DR KEGG; ath:AT5G49730; -.
DR Araport; AT5G49730; -.
DR TAIR; locus:2157027; AT5G49730.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_014777_0_0_1; -.
DR InParanoid; Q8RWS6; -.
DR OrthoDB; 190356at2759; -.
DR PhylomeDB; Q8RWS6; -.
DR PRO; PR:Q8RWS6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RWS6; baseline and differential.
DR Genevisible; Q8RWS6; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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 GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
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 Cell membrane; Electron transport; FAD; Flavoprotein; Heme; Ion transport;
KW Iron; Membrane; Metal-binding; NAD; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..738
FT /note="Ferric reduction oxidase 6"
FT /id="PRO_0000413204"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..49
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 50..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..90
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 91..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..146
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 147..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..236
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 237..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..312
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 313..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 356..564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..587
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 588..602
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..625
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 626..738
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 178..299
FT /note="Ferric oxidoreductase"
FT DOMAIN 328..445
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
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:0000305"
FT BINDING 228
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 289
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 302
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 377..380
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 437..440
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 738 AA; 83458 MW; DF0E91C503383FA8 CRC64;
MDDYETPLLS KDSSSSSSVI TSSLKWILKV VMSMIFVTWV VFLMMMYPEQ LGDDFLTFVS
SKTFLGTTGT MFLIFSCPIL VISVLASLYL IISGEDKVFT KKKISKFPRF RLWTFPVLVD
GPFGVVSAAE FLGIMVFSVF FLWSIYAYTL RNLDLLERFH VLPKNRSILL LEVTGLRLGM
IGLLCMVFLF LPISRGSILL RLIDIPFEHA TRYHVWLGHI TMAFFSLHGL CYVVGWIIQG
QLLELIFSWN AIGIAILPGV ISLVAGLLMW VTSLHTVRKN YFELFFYTHQ LYIVFIVFLA
LHVGDYMFSI VAGGIFLFIL DRFLRFCQSR RTVDVISAKS LPCGTLELVL SKPPNMRYNA
LSFIFLQVRE LSWLQWHPFS VSSSPLDGNH HVAVLIKVLG GWTAKLRDQL SNLYEAENQD
QLISPQSYPK ITTCVEGPYG HESPYHLAYE NLVLVAGGIG ITPFFAILSD ILHRKRDGKA
CLPSKVLVVW AIKNSDELSL LSAIDIPSIC PFFSKKLNLE IHIYITRQSE PRLEDGMVHK
VVHPSVKLPR TNGCSMSVLV GTGDNIWSGL YLIISTIGFI SMITLLDIFY IKRYNITTWW
YKGLLFVGCM VASVLIFGGL VVVFWHRWEH KTGEVEANGN DKVDLNGEET HNPSAAELKG
LAIEEDVQNY TTIRYGTRPA FREIFESLNG KWGSVDVGVI VCGPATLQTT VAKEIRSHSI
WRSANHPLFH FNSHSFDL
