FENR_SYNY3
ID FENR_SYNY3 Reviewed; 413 AA.
AC Q55318; P74364;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ferredoxin--NADP reductase;
DE Short=FNR;
DE EC=1.18.1.2;
GN Name=petH {ECO:0000303|PubMed:9484476}; OrderedLocusNames=slr1643;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROBABLE COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=9484476; DOI=10.1023/a:1005935819038;
RA van Thor J.J., Hellingwerf K.J., Matthijs H.C.P.;
RT "Characterization and transcriptional regulation of the Synechocystis PCC
RT 6803 petH gene, encoding ferredoxin-NADP+ oxidoreductase: involvement of a
RT novel type of divergent operator.";
RL Plant Mol. Biol. 36:353-363(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP PROTEIN SEQUENCE OF 1-12 AND 66-74, SUBUNIT, AND ACETYLATION AT MET-1.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=31015331; DOI=10.1128/mbio.00669-19;
RA Liu H., Weisz D.A., Zhang M.M., Cheng M., Zhang B., Zhang H.,
RA Gerstenecker G.S., Pakrasi H.B., Gross M.L., Blankenship R.E.;
RT "Phycobilisomes Harbor FNRL in Cyanobacteria.";
RL MBio 10:0-0(2019).
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 Evidence={ECO:0000305|PubMed:9484476};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for NADPH (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:9484476};
CC Vmax=110 umol/min/mg enzyme toward NADPH (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:9484476};
CC Note=The enzyme was overproduced in E.coli.
CC {ECO:0000269|PubMed:9484476};
CC -!- SUBUNIT: Purifies with both the classic phycobilisome (PBS)
CC supercomplex (CpcG-PBS) and a photosystem I-associated PBS called CpcL-
CC PBS; it accumulates to a higher level in CpcL-PBS. In both PBS it can
CC be cross-linked to both phycocyanin subunits.
CC {ECO:0000269|PubMed:31015331}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane
CC protein; Cytoplasmic side. Note=May be bound to the thylakoid membrane
CC or anchored to the thylakoid-bound phycobilisomes.
CC -!- INDUCTION: By light, and also by 0.55 M NaCl.
CC {ECO:0000269|PubMed:9484476}.
CC -!- PTM: Acetylated at the N-terminus; 6% of protein in CpcG-PBS and 12% of
CC protein in CpcL-PBS is acetylated. {ECO:0000269|PubMed:31015331}.
CC -!- DISRUPTION PHENOTYPE: Essential for growth.
CC {ECO:0000269|PubMed:9484476}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; X94297; CAA63961.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18459.1; -; Genomic_DNA.
DR PIR; S76200; S76200.
DR AlphaFoldDB; Q55318; -.
DR SMR; Q55318; -.
DR IntAct; Q55318; 1.
DR MINT; Q55318; -.
DR STRING; 1148.1653546; -.
DR PaxDb; Q55318; -.
DR EnsemblBacteria; BAA18459; BAA18459; BAA18459.
DR KEGG; syn:slr1643; -.
DR eggNOG; COG0369; Bacteria.
DR InParanoid; Q55318; -.
DR OMA; GKAWLFM; -.
DR PhylomeDB; Q55318; -.
DR BioCyc; MetaCyc:MON-21694; -.
DR BRENDA; 1.18.1.2; 382.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR008213; CpcD-like_dom.
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; PF01383; CpcD; 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 SMART; SM01094; CpcD; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51441; CPCD_LIKE; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Antenna complex; Direct protein sequencing; FAD; Flavoprotein;
KW Membrane; NADP; Oxidoreductase; Phycobilisome; Reference proteome;
KW Thylakoid.
FT CHAIN 1..413
FT /note="Ferredoxin--NADP reductase"
FT /id="PRO_0000167638"
FT DOMAIN 18..76
FT /note="CpcD-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00771"
FT DOMAIN 133..256
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 74..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 192..195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 213..215
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 230..232
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 303..304
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 333..334
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 343..347
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 372..373
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000305|PubMed:31015331"
FT CONFLICT 182
FT /note="E -> K (in Ref. 1; CAA63961)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="D -> S (in Ref. 1; CAA63961)"
FT /evidence="ECO:0000305"
FT CONFLICT 347..350
FT /note="QHRV -> STGL (in Ref. 1; CAA63961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 46360 MW; FF33709639F0CAA8 CRC64;
MYSPGYVATS SRQSDAGNRL FVYEVIGLSQ STMTDGLDYP IRRSGSTFIT VPLKRMNQEM
RRITRMGGKI VSIKPLEGDS PLPHTEGIAK PSQSEGSGSE AVANPAPESN KTMTTTPKEK
KADDIPVNIY RPKTPYIGKV LENYPLVREG AIGTVQHLTF DLSAGDLRYL EGQSIGIIPP
GEDDKGKPHK LRLYSIASTR HGDFGDDKTV SLCVRQLEYQ NEAGETVQGV CSTYLCNIKE
GDDIAITGPV GKEMLLPPDE DANIVMLATG TGIAPFRAFL WRMFKEQHED YKFKGLAWLI
FGIPKSENIL YKDDLEKMAA EFPDNFRLTY AISREQQNAE GGRMYIQHRV AENAEELWNL
MQNPKTHTYM CGLKGMEPGI DEAFTALAEQ NGKEWTTFQR EMKKEHRWHV ETY
