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Database: UniProt
Entry: A0A239TSG9_9STAP
LinkDB: A0A239TSG9_9STAP
Original site: A0A239TSG9_9STAP 
ID   A0A239TSG9_9STAP        Unreviewed;       345 AA.
AC   A0A239TSG9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
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   ORFNames=SPI02_21790 {ECO:0000313|EMBL:GEP85594.1};
OS   Staphylococcus piscifermentans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=70258 {ECO:0000313|EMBL:GEP85594.1, ECO:0000313|Proteomes:UP000321736};
RN   [1] {ECO:0000313|EMBL:GEP85594.1, ECO:0000313|Proteomes:UP000321736}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 109625 {ECO:0000313|EMBL:GEP85594.1,
RC   ECO:0000313|Proteomes:UP000321736};
RA   Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT   "Whole genome shotgun sequence of Staphylococcus piscifermentans NBRC
RT   109625.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GEP85594.1}.
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DR   EMBL; BKAR01000035; GEP85594.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239TSG9; -.
DR   OrthoDB; 9806179at2; -.
DR   Proteomes; UP000321736; Unassembled WGS sequence.
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..290
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;  38133 MW;  C77EBAA7CBB59C73 CRC64;
     MKDVTIIGGG PAGLYASFYA GLRGMSVRLI DVQDKLGGKM QLYPEKIIWD IGGIAPKPCY
     QIIEDMIEQG LHFQPEVNLE TRVTNIEKLG ERHFKITTDN DESFESKSVI IAVGGGIINP
     KPLDIKDAER YQISNLHYVV QKLSRFAGKK VVISGAGNAA LDWACDIAPY AESVRLVYRK
     DKMKGYEGTQ AKLCDRDVIL HPNSQITALI GDDQHEKIKE IVLENSETGE AETIPVDEVI
     ISHGFDIENP LLEEAATQLE MENEYQIKGQ GNTQTSIEGI FACGDIIHHG AKAHLIASAF
     SDAGNAANLA KLYIEPEAAE EGYVSSHNEI FKEDNKEIIE KYNQE
//
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