FENR_SYNP2
ID FENR_SYNP2 Reviewed; 402 AA.
AC P31973; B1XII6;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ferredoxin--NADP reductase;
DE Short=FNR;
DE EC=1.18.1.2;
GN Name=petH; OrderedLocusNames=SYNPCC7002_A0853;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP CHARACTERIZATION.
RX PubMed=1554697; DOI=10.1021/bi00127a009;
RA Schluchter W.M., Bryant D.A.;
RT "Molecular characterization of ferredoxin-NADP+ oxidoreductase in
RT cyanobacteria: cloning and sequence of the petH gene of Synechococcus sp.
RT PCC 7002 and studies on the gene product.";
RL Biochemistry 31:3092-3102(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RX PubMed=8501038; DOI=10.1128/jb.175.11.3343-3352.1993;
RA Schluchter W.M., Zhao J., Bryant D.A.;
RT "Isolation and characterization of the ndhF gene of Synechococcus sp.
RT strain PCC 7002 and initial characterization of an interposon mutant.";
RL J. Bacteriol. 175:3343-3352(1993).
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: 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 -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; M86234; AAA27323.1; -; Genomic_DNA.
DR EMBL; CP000951; ACA98857.1; -; Genomic_DNA.
DR EMBL; M99378; AAA27310.1; -; Genomic_DNA.
DR RefSeq; WP_012306481.1; NC_010475.1.
DR PDB; 2B5O; X-ray; 2.50 A; A/B=1-402.
DR PDBsum; 2B5O; -.
DR AlphaFoldDB; P31973; -.
DR SMR; P31973; -.
DR STRING; 32049.SYNPCC7002_A0853; -.
DR EnsemblBacteria; ACA98857; ACA98857; SYNPCC7002_A0853.
DR KEGG; syp:SYNPCC7002_A0853; -.
DR eggNOG; COG0369; Bacteria.
DR HOGENOM; CLU_053066_0_0_3; -.
DR OMA; GKAWLFM; -.
DR EvolutionaryTrace; P31973; -.
DR Proteomes; UP000001688; 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 3D-structure; Antenna complex; Direct protein sequencing; FAD;
KW Flavoprotein; Membrane; NADP; Oxidoreductase; Phycobilisome;
KW Reference proteome; Thylakoid.
FT CHAIN 1..402
FT /note="Ferredoxin--NADP reductase"
FT /id="PRO_0000167637"
FT DOMAIN 18..74
FT /note="CpcD-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00771"
FT DOMAIN 120..245
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 80..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179..182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 200..202
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 202
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 218..220
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 260
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 292..293
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 322..323
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 332..336
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 361..362
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2B5O"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:2B5O"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:2B5O"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:2B5O"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:2B5O"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:2B5O"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:2B5O"
FT TURN 187..192
FT /evidence="ECO:0007829|PDB:2B5O"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:2B5O"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:2B5O"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:2B5O"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2B5O"
FT HELIX 218..224
FT /evidence="ECO:0007829|PDB:2B5O"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:2B5O"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:2B5O"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:2B5O"
FT HELIX 263..273
FT /evidence="ECO:0007829|PDB:2B5O"
FT STRAND 284..294
FT /evidence="ECO:0007829|PDB:2B5O"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:2B5O"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:2B5O"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:2B5O"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:2B5O"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:2B5O"
FT HELIX 335..341
FT /evidence="ECO:0007829|PDB:2B5O"
FT HELIX 343..350
FT /evidence="ECO:0007829|PDB:2B5O"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:2B5O"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:2B5O"
FT HELIX 366..379
FT /evidence="ECO:0007829|PDB:2B5O"
FT HELIX 384..393
FT /evidence="ECO:0007829|PDB:2B5O"
FT STRAND 397..401
FT /evidence="ECO:0007829|PDB:2B5O"
SQ SEQUENCE 402 AA; 45015 MW; 5203060291BAFAE7 CRC64;
MYGITSTANS TGNQSYANRL FIYEVVGLGG DGRNENSLVR KSGTTFITVP YARMNQEMQR
ITKLGGKIVS IRPAEDAAQI VSEGQSSAQA SAQSPMASST KIVHPKTTDT SVPVNIYRPK
TPFLGKCIEN YELVDEGGSG TVRHVTFDIS EGDLRYLEGQ SIGIIPPGED KNGKPHKLRL
YSIASTRHGD MEDNKTVSLC VRQLEYQDPE SGETVYGVCS TYLCNLPVGT DDVKITGPVG
KEMLLPDDED ATVVMLATGT GIAPFRAFLW RMFKEQHEDY KFKGKAWLIF GVPYTANILY
KDDFEKMAAE NPDNFRLTYA ISREQKTADG GKVYVQSRVS EYADELFEMI QKPNTHVYMC
GLKGMQPPID ETFTAEAEKR GLNWEEMRRS MKKEHRWHVE VY
