FNRR2_ARATH
ID FNRR2_ARATH Reviewed; 382 AA.
AC Q9S9P8; Q3ED46; Q3ED47; Q8LA56;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ferredoxin--NADP reductase, root isozyme 2, chloroplastic;
DE EC=1.18.1.2;
DE AltName: Full=Root FNR 2;
DE Short=AtRFNR2;
DE Flags: Precursor;
GN Name=RFNR2; Synonyms=PETH4; OrderedLocusNames=At1g30510;
GN ORFNames=F26G16.13;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INDUCTION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS
RP SPECTROMETRY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RA Hanke G.T., Okutani S., Satomi Y., Takao T., Suzuki A., Hase T.;
RT "Multiple iso-proteins of FNR in Arabidopsis: evidence for different
RT contributions to chloroplast function and nitrogen assimilation.";
RL Plant Cell Environ. 28:1146-1157(2005).
CC -!- FUNCTION: Maintains the supply of reduced ferredoxin under non-
CC photosynthetic conditions. {ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.18.1.2;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9S9P8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9S9P8-2; Sequence=VSP_031939;
CC Name=3;
CC IsoId=Q9S9P8-3; Sequence=VSP_031938;
CC -!- TISSUE SPECIFICITY: Expressed in shoots and roots. More abundant in
CC roots than RFNR1. {ECO:0000269|Ref.5}.
CC -!- INDUCTION: Up-regulated by nitrate in roots while down-regulated in
CC shoots. {ECO:0000269|Ref.5}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AC009917; AAF19753.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31235.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31236.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31237.1; -; Genomic_DNA.
DR EMBL; AF424594; AAL11588.1; -; mRNA.
DR EMBL; AY140017; AAM98159.1; -; mRNA.
DR EMBL; BT008468; AAP37827.1; -; mRNA.
DR EMBL; AY088018; AAM65564.1; -; mRNA.
DR PIR; B86430; B86430.
DR RefSeq; NP_564355.1; NM_102787.1. [Q9S9P8-2]
DR RefSeq; NP_849734.1; NM_179403.4. [Q9S9P8-1]
DR RefSeq; NP_973942.1; NM_202213.1. [Q9S9P8-3]
DR AlphaFoldDB; Q9S9P8; -.
DR SMR; Q9S9P8; -.
DR BioGRID; 25165; 3.
DR STRING; 3702.AT1G30510.2; -.
DR PaxDb; Q9S9P8; -.
DR PRIDE; Q9S9P8; -.
DR ProteomicsDB; 230556; -. [Q9S9P8-1]
DR EnsemblPlants; AT1G30510.1; AT1G30510.1; AT1G30510. [Q9S9P8-2]
DR EnsemblPlants; AT1G30510.2; AT1G30510.2; AT1G30510. [Q9S9P8-1]
DR EnsemblPlants; AT1G30510.3; AT1G30510.3; AT1G30510. [Q9S9P8-3]
DR GeneID; 839930; -.
DR Gramene; AT1G30510.1; AT1G30510.1; AT1G30510. [Q9S9P8-2]
DR Gramene; AT1G30510.2; AT1G30510.2; AT1G30510. [Q9S9P8-1]
DR Gramene; AT1G30510.3; AT1G30510.3; AT1G30510. [Q9S9P8-3]
DR KEGG; ath:AT1G30510; -.
DR Araport; AT1G30510; -.
DR TAIR; locus:2028145; AT1G30510.
DR eggNOG; KOG1158; Eukaryota.
DR InParanoid; Q9S9P8; -.
DR OrthoDB; 817123at2759; -.
DR PhylomeDB; Q9S9P8; -.
DR BioCyc; ARA:AT1G30510-MON; -.
DR PRO; PR:Q9S9P8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S9P8; baseline and differential.
DR Genevisible; Q9S9P8; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR015701; FNR.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR035442; FNR_plant_Cyanobacteria.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43314; PTHR43314; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF501178; FNR-PetH; 1.
DR PIRSF; PIRSF000361; Frd-NADP+_RD; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Coiled coil; Disulfide bond;
KW Electron transport; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Phosphoprotein; Photosynthesis; Plastid; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..64
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 65..382
FT /note="Ferredoxin--NADP reductase, root isozyme 2,
FT chloroplastic"
FT /id="PRO_0000322575"
FT DOMAIN 97..225
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 235..253
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW6"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW6"
FT DISULFID 200..205
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..65
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_031938"
FT VAR_SEQ 29
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_031939"
FT CONFLICT 320
FT /note="I -> V (in Ref. 4; AAM65564)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 42789 MW; 66C4950471D1A6F4 CRC64;
MSHSAVSQAG AVSVSIENQR SLRRSVFKQN NSISFNSKSW SSSLALNQKT TSIRDGKRYP
STTICMSVQQ TSSSKVTVSP IELEDPKDPP LNLYKPKESY TAKIVSVERV VGPKAPGETC
HIVIDHDGNL PYWEGQSYGV IPPGENPKKP GAPHNVRLYS IASTRYGDFF DGKTASLCVR
RAVYYDPETG KEDPSKNGVC SNFLCDSKPG DKIQITGPSG KVMLLPESDP NATHIMIATG
TGVAPYRGYL RRMFMENVPN KTFSGLAWLF LGVANTDSLL YDEEFTKYLK DHPDNFRFDK
ALSREEKNKK GGKMYVQDKI EEYSDEIFKL LDNGAHIYFC GLKGMMPGIQ DTLKRVAEER
GESWDLKLSQ LRKNKQWHVE VY
