FRO7_ARATH
ID FRO7_ARATH Reviewed; 747 AA.
AC Q3KTM0; Q9LT99;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Ferric reduction oxidase 7, chloroplastic;
DE Short=AtFRO7;
DE EC=1.16.1.7;
DE AltName: Full=Ferric-chelate reductase 7;
DE Flags: Precursor;
GN Name=FRO7; OrderedLocusNames=At5g49740; ORFNames=K2I5.10;
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;
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 [5]
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 [6]
RP 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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
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 [8]
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 mobilization from
CC the cytosol into the chloroplast. May participate in the transport of
CC electrons to a Fe(3+) ion via FAD and heme intermediates. Might be
CC involved iron homeostasis in trichomes. {ECO:0000269|PubMed:16006655,
CC ECO:0000269|PubMed:18647837}.
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: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in shoots, flowers and siliques. Detected
CC in cotyledons, leaves and trichomes, but not in roots.
CC {ECO:0000269|PubMed:16006655, ECO:0000269|PubMed:16362328,
CC ECO:0000269|PubMed:18647837}.
CC -!- DEVELOPMENTAL STAGE: Expressed during cell or organ differentiation.
CC {ECO:0000269|PubMed:16489134}.
CC -!- INDUCTION: Up-regulated in shoots by iron deficiency and down-regulated
CC in shoots by copper deficiency. {ECO:0000269|PubMed:16362328}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions. Reduced photosynthetic electron transport efficiency,
CC chloroplast ferric chelate reductase activity and iron content.
CC Seedling lethal when grown in alkaline soil.
CC {ECO:0000269|PubMed:18647837}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA98162.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY912280; AAX92640.1; -; mRNA.
DR EMBL; AB025613; BAA98162.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95852.1; -; Genomic_DNA.
DR EMBL; AK227087; BAE99139.1; -; mRNA.
DR RefSeq; NP_199785.2; NM_124352.4.
DR AlphaFoldDB; Q3KTM0; -.
DR SMR; Q3KTM0; -.
DR STRING; 3702.AT5G49740.1; -.
DR PaxDb; Q3KTM0; -.
DR PRIDE; Q3KTM0; -.
DR ProteomicsDB; 230549; -.
DR EnsemblPlants; AT5G49740.1; AT5G49740.1; AT5G49740.
DR GeneID; 835037; -.
DR Gramene; AT5G49740.1; AT5G49740.1; AT5G49740.
DR KEGG; ath:AT5G49740; -.
DR Araport; AT5G49740; -.
DR TAIR; locus:2157032; AT5G49740.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_014777_0_0_1; -.
DR InParanoid; Q3KTM0; -.
DR OrthoDB; 190356at2759; -.
DR PhylomeDB; Q3KTM0; -.
DR BioCyc; ARA:AT5G49740-MON; -.
DR BioCyc; MetaCyc:AT5G49740-MON; -.
DR BRENDA; 1.16.1.7; 399.
DR PRO; PR:Q3KTM0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q3KTM0; baseline and differential.
DR Genevisible; Q3KTM0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
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:0009536; C:plastid; HDA:TAIR.
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 GO; GO:0009767; P:photosynthetic electron transport chain; IMP: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 Chloroplast; Electron transport; FAD; Flavoprotein; Heme; Ion transport;
KW Iron; Membrane; Metal-binding; NAD; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..28
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 29..747
FT /note="Ferric reduction oxidase 7, chloroplastic"
FT /id="PRO_0000413205"
FT TRANSMEM 37..56
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 81..99
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 132..155
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 222..245
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 297..321
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 574..596
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 612..634
FT /note="Helical"
FT /evidence="ECO:0000250"
FT DOMAIN 187..308
FT /note="Ferric oxidoreductase"
FT DOMAIN 337..454
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250"
FT BINDING 237
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 298
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 311
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 386..389
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 446..449
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 747 AA; 84126 MW; BB09E91DDC5F5207 CRC64;
MDDHETPLLS KDLSSSSSSS SSSSSVVVSS LKWILKVVMS VIFVTWVVFL MMYPGSLGDQ
ILTNWRAISS NTLFGLTGSM FLIFSGPILV IAILASLYLI ISGEETVFTK KKITKFPRFR
LWTFPVLVDG PFGVVSAAEF LGIMVFSVFF LWAIYAYTLR NLNVLDYFHV LPNNRSIFLL
ELTGLRFGMI GLLCMVFLFL PISRGSILLR LIDIPFEHAT RYHVWLGHIT MTFFSLHGLC
YVVGWTIQGQ LLELLFEWKA TGIAVLPGVI SLVAGLLMWV TSLHTVRKNY FELFFYTHQL
YIVFVVFLAL HVGDYLFSIV AGGIFLFILD RFLRFYQSRR TVDVISAKSL PCGTLELVLS
KPPNMRYNAL SFIFLQVKEL SWLQWHPFSV SSSPLDGNHH VAVLIKVLGG WTAKLRDQLS
TLYEAENQDQ LISPESYPKI TTCVEGPYGH ESPYHLAYEN LVLVAGGIGI TPFFAILSDI
LHRKRDGKDC LPGKVLVVWA IKNSDELSLL SAIDIPSICH FFSKKLNLEI HIYVTRQSEP
CLEDGMVHKV VHPSVKTPWT NGCSMSVLVG TGDNIWSGLY LIISTIGFIA MITLVDIFYI
NKYNITTWWY KGLLFVVCMV ASVLIFGGLV VVFWHRWEHK TGEVEANGND KVDLNGEETH
NPSAAELKGL AIEEDVQNYT TIRYGTRPAF REIFESLNGK WGSVDVGVIV CGPATLQTTV
AKEIRSHSIW RSANHPLFHF NSHSFDL
