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FENR2_ORYSJ
ID   FENR2_ORYSJ             Reviewed;         366 AA.
AC   Q6ZFJ3;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Ferredoxin--NADP reductase, leaf isozyme 2, chloroplastic;
DE            EC=1.18.1.2 {ECO:0000250|UniProtKB:Q9FKW6};
DE   AltName: Full=Leaf FNR 2 {ECO:0000303|PubMed:26941088};
DE            Short=FNR-2 {ECO:0000303|PubMed:26941088};
DE            Short=Os-LFNR2 {ECO:0000303|PubMed:26941088};
DE   Flags: Precursor;
GN   Name=LFNR2 {ECO:0000303|PubMed:26941088};
GN   OrderedLocusNames=LOC_Os02g01340 {ECO:0000305}, Os02g0103800 {ECO:0000305};
GN   ORFNames=OJ1435_F07.32-2 {ECO:0000312|EMBL:BAD07827.1},
GN   OsJ_05011 {ECO:0000312|EMBL:EAZ21407.1},
GN   OSNPB_020103800 {ECO:0000312|EMBL:BAS76543.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [5]
RP   INTERACTION WITH LIR1 AND TIC62, AND DISULFIDE BOND.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=26941088; DOI=10.1105/tpc.15.01027;
RA   Yang C., Hu H., Ren H., Kong Y., Lin H., Guo J., Wang L., He Y., Ding X.,
RA   Grabsztunowicz M., Mulo P., Chen T., Liu Y., Wu Z., Wu Y., Mao C., Wu P.,
RA   Mo X.;
RT   "LIGHT-INDUCED RICE1 regulates light-dependent attachment of LEAF-TYPE
RT   FERREDOXIN-NADP+ OXIDOREDUCTASE to the thylakoid membrane in rice and
RT   Arabidopsis.";
RL   Plant Cell 28:712-728(2016).
CC   -!- FUNCTION: Plays a key role in regulating the relative amounts of cyclic
CC       and non-cyclic electron flow to meet the demands of the plant for ATP
CC       and reducing power. {ECO:0000250|UniProtKB:Q9FKW6}.
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         Evidence={ECO:0000250|UniProtKB:Q9FKW6};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q9FKW6};
CC   -!- PATHWAY: Energy metabolism; photosynthesis.
CC       {ECO:0000250|UniProtKB:Q9FKW6}.
CC   -!- SUBUNIT: Heterodimer with LFNR1 (By similarity). Component of high
CC       molecular weight thylakoid LFNRs-containing protein complexes
CC       containing LIR1, LFNR1, LFNR2, TIC62 and TROL proteins. Interacts
CC       directly with LIR1 and TIC62; LIR1 increases the affinity of LFNR1 and
CC       LFNR2 for TIC62 (PubMed:26941088). {ECO:0000250|UniProtKB:Q9FKW6,
CC       ECO:0000269|PubMed:26941088}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000250|UniProtKB:Q9FKW6}. Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250|UniProtKB:Q9FKW6}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9FKW6}; Stromal side
CC       {ECO:0000250|UniProtKB:Q9FKW6}.
CC   -!- PTM: May form interchain disulfide bonds with LIR1.
CC       {ECO:0000269|PubMed:26941088}.
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AP004187; BAD07827.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS76543.1; -; Genomic_DNA.
DR   EMBL; CM000139; EAZ21407.1; -; Genomic_DNA.
DR   EMBL; AK065309; BAG89459.1; -; mRNA.
DR   RefSeq; XP_015625198.1; XM_015769712.1.
DR   AlphaFoldDB; Q6ZFJ3; -.
DR   SMR; Q6ZFJ3; -.
DR   STRING; 4530.OS02T0103800-01; -.
DR   PaxDb; Q6ZFJ3; -.
DR   PRIDE; Q6ZFJ3; -.
DR   EnsemblPlants; Os02t0103800-01; Os02t0103800-01; Os02g0103800.
DR   EnsemblPlants; Os02t0103800-03; Os02t0103800-03; Os02g0103800.
DR   GeneID; 4328000; -.
DR   Gramene; Os02t0103800-01; Os02t0103800-01; Os02g0103800.
DR   Gramene; Os02t0103800-03; Os02t0103800-03; Os02g0103800.
DR   KEGG; osa:4328000; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   InParanoid; Q6ZFJ3; -.
DR   OrthoDB; 817123at2759; -.
DR   BRENDA; 1.18.1.2; 8948.
DR   UniPathway; UPA00091; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   ExpressionAtlas; Q6ZFJ3; baseline and differential.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0098807; C:chloroplast thylakoid membrane protein complex; IDA:UniProtKB.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniPathway.
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   Chloroplast; Disulfide bond; Electron transport; FAD; Flavoprotein;
KW   Membrane; NADP; Oxidoreductase; Phosphoprotein; Photosynthesis; Plastid;
KW   Reference proteome; Thylakoid; Transit peptide; Transport.
FT   TRANSIT         1..48
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..366
FT                   /note="Ferredoxin--NADP reductase, leaf isozyme 2,
FT                   chloroplastic"
FT                   /id="PRO_0000442379"
FT   DOMAIN          87..209
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         145..148
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10933"
FT   BINDING         148
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P10933"
FT   BINDING         166..168
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10933"
FT   BINDING         168
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P10933"
FT   BINDING         172
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10933"
FT   BINDING         183..185
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10933"
FT   BINDING         224
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P00455"
FT   BINDING         224
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P10933"
FT   BINDING         256..257
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P10933"
FT   BINDING         286..287
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P10933"
FT   BINDING         296
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P10933"
FT   BINDING         325..326
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P10933"
FT   BINDING         364
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P10933"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FKW6"
FT   MOD_RES         216
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FKW6"
FT   DISULFID        184..189
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   366 AA;  40665 MW;  01C5BCE33EF30F09 CRC64;
     MAAVNTVSSL PCSKAGAAVA GGAPRPSTCS VFYPPRCWSK RSSGNGVRAQ ASTTETTAAP
     AAEVTTKVEK VSKKQVDGVV TNKYRPKEPY TGRCLLNTRI TGDDAPGETW HMVFSTDGEI
     PYREGQSIGV IPDGIDKNGK PHKLRLYSIA SSAIGDFADS KTVSLCVKRL VYTNDQGEIV
     KGVCSNFLCD LKPGSDVKIT GPVGKEMLMP KDPNATIIML GTGTGIAPFR SFLWKMFFEE
     HDDYKFNGLA WLFLGVPTSS TLLYREEFER MKEIAPERFR LDFAVSREQT NAAGEKMYIQ
     TRMAEYKDEL WELLKKDNTY VYMCGLKGME KGIDDIMIDL AAKDGIDWLD YKKQLKKSEQ
     WNVEVY
 
 
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