FENR_STAA8
ID FENR_STAA8 Reviewed; 344 AA.
AC Q2FVP8;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Ferredoxin--NADP reductase {ECO:0000255|HAMAP-Rule:MF_01685};
DE Short=FNR {ECO:0000255|HAMAP-Rule:MF_01685};
DE Short=Fd-NADP(+) reductase {ECO:0000255|HAMAP-Rule:MF_01685};
DE EC=1.18.1.2 {ECO:0000255|HAMAP-Rule:MF_01685};
GN OrderedLocusNames=SAOUHSC_02654;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01685};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01685};
CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01685};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01685}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01685}.
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DR EMBL; CP000253; ABD31662.1; -; Genomic_DNA.
DR RefSeq; WP_000655971.1; NZ_LS483365.1.
DR RefSeq; YP_501116.1; NC_007795.1.
DR PDB; 6A4J; X-ray; 3.40 A; A/B=1-344.
DR PDBsum; 6A4J; -.
DR AlphaFoldDB; Q2FVP8; -.
DR SMR; Q2FVP8; -.
DR STRING; 1280.SAXN108_2626; -.
DR EnsemblBacteria; ABD31662; ABD31662; SAOUHSC_02654.
DR GeneID; 3921216; -.
DR KEGG; sao:SAOUHSC_02654; -.
DR PATRIC; fig|93061.5.peg.2401; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_5_9; -.
DR OMA; LEQCAPF; -.
DR PRO; PR:Q2FVP8; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 2.
DR HAMAP; MF_01685; FENR2; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR022890; Fd--NADP_Rdtase_type_2.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..344
FT /note="Ferredoxin--NADP reductase"
FT /id="PRO_0000364944"
FT BINDING 12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 31
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 326
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6A4J"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:6A4J"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6A4J"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:6A4J"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:6A4J"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:6A4J"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6A4J"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6A4J"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:6A4J"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:6A4J"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:6A4J"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:6A4J"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:6A4J"
FT HELIX 296..314
FT /evidence="ECO:0007829|PDB:6A4J"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:6A4J"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:6A4J"
FT HELIX 332..340
FT /evidence="ECO:0007829|PDB:6A4J"
SQ SEQUENCE 344 AA; 38230 MW; 46E1A319359751D3 CRC64;
MKDVTIIGGG PSGLYASFYA GLRDMSVRLI DVQSELGGKM RIYPEKIIWD IGGIAPKPCH
EILKDTIKQG LYFKPEVHLN ERVVDIRKKA ERHFEVETEA GEIYTSKAVI IAIGAGIINP
KQLDVKGVER YQLTNLHYVV QSYRRFKDKD VLISGGGNTA LDWAHDIAKI AKSVTVVYRK
EDVSGHEAMK TLVTDLNVKL CPKTRIKYLV GNDDETHISE VVLEHVESGD RHTVKFDDVI
ISHGFDRCNT LLSETSSKLD MHDDCRVKGF GNTTTSIPGI YACGDIVYHD AKSHLIASAF
SDGANAANLA KTYIQPDANA EGYVSSHHEV FKEANKTIVN KHLY
