ID B9DLB5_STACT Unreviewed; 345 AA.
AC B9DLB5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Ferredoxin--NADP reductase {ECO:0000256|HAMAP-Rule:MF_01685};
DE Short=FNR {ECO:0000256|HAMAP-Rule:MF_01685};
DE Short=Fd-NADP(+) reductase {ECO:0000256|HAMAP-Rule:MF_01685};
DE EC=1.18.1.2 {ECO:0000256|HAMAP-Rule:MF_01685};
GN OrderedLocusNames=Sca_1872 {ECO:0000313|EMBL:CAL28778.1};
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513 {ECO:0000313|EMBL:CAL28778.1, ECO:0000313|Proteomes:UP000000444};
RN [1] {ECO:0000313|EMBL:CAL28778.1, ECO:0000313|Proteomes:UP000000444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300 {ECO:0000313|EMBL:CAL28778.1,
RC ECO:0000313|Proteomes:UP000000444};
RX PubMed=19060169; DOI=10.1128/AEM.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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:0000256|HAMAP-
CC Rule:MF_01685};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01685};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_01685};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01685}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family.
CC {ECO:0000256|HAMAP-Rule:MF_01685}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01685}.
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DR EMBL; AM295250; CAL28778.1; -; Genomic_DNA.
DR RefSeq; WP_015901114.1; NC_012121.1.
DR AlphaFoldDB; B9DLB5; -.
DR GeneID; 60544414; -.
DR KEGG; sca:SCA_1872; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_5_9; -.
DR OrthoDB; 9806179at2; -.
DR BioCyc; SCAR396513:SCA_RS09500-MONOMER; -.
DR Proteomes; UP000000444; 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 Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 PANTHER; PTHR48105:SF18; FERREDOXIN--NADP REDUCTASE; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01685};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01685}; NADP {ECO:0000256|HAMAP-Rule:MF_01685};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01685}.
FT DOMAIN 2..291
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 31
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 326
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
SQ SEQUENCE 345 AA; 37938 MW; F7C663A9F8A4B24D CRC64;
MKDVTIIGGG PAGLYASFYA GLRGMSVRLI DVQDKLGGKM QLYPEKIIWD IGGIGPKPCY
QIIEDMIGQG LHFQPEVNLE TRVTNIEKLG DCHFEITTDK DEVFETKSVI IAVGGGIINP
KPLDIKDAER YQISNLHYVV QKLSRFSGKK VVISGAGNAA LDWACDIAPY AESVRLVYRK
DKMKGYEGTQ AKLCDNGIKL HPNSQITALI GDDQHEKIKE IVLENSETGE AETIPVDEVI
ISHGFDIENP LLEEAATQLE MENDYQIKGQ GNTQTSIDGI FACGDVIHHG AKAHLIASAF
SDAGNAANLA KQYIEPEAAE EGYVSSHNEI FKEDNKEIIE KYNQQ
//
