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Entry: A0A0Q7SI04_9BACL
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ID   A0A0Q7SI04_9BACL        Unreviewed;       340 AA.
AC   A0A0Q7SI04;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, 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=ASD24_08350 {ECO:0000313|EMBL:KQY87829.1};
OS   Paenibacillus sp. Root52.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736552 {ECO:0000313|EMBL:KQY87829.1, ECO:0000313|Proteomes:UP000051734};
RN   [1] {ECO:0000313|Proteomes:UP000051734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root52 {ECO:0000313|Proteomes:UP000051734};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY87829.1, ECO:0000313|Proteomes:UP000051734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root52 {ECO:0000313|EMBL:KQY87829.1,
RC   ECO:0000313|Proteomes:UP000051734};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQY87829.1}.
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DR   EMBL; LMFO01000012; KQY87829.1; -; Genomic_DNA.
DR   RefSeq; WP_056696859.1; NZ_LMFO01000012.1.
DR   AlphaFoldDB; A0A0Q7SI04; -.
DR   STRING; 1736552.ASD24_08350; -.
DR   OrthoDB; 9806179at2; -.
DR   Proteomes; UP000051734; 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|HAMAP-Rule:MF_01685};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01685};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01685};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01685}.
FT   DOMAIN          7..299
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   BINDING         36
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT   BINDING         48
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT   BINDING         88
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT   BINDING         284
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT   BINDING         325
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
SQ   SEQUENCE   340 AA;  37924 MW;  18447C69FE1DF4AC CRC64;
     MREEDIYDVT IIGGGPAGMY AAFYAGMREM KVKIIEGKDQ LGGFLHTYAE KTIWDVGGLP
     PMKCSKLIEW LVQQANTFNP TVIFNRQMEC FSRLENGILA LYTAEGEIHY TRTMIIAVGR
     GVAEIQRLEL QESNDNEPIN LHYTVQNPEY FAGKRVLVSG GGNSAVDWAI ELAKVAQRVV
     VIHRQSEFRA MERNVSDMHE IADVRTPYQI TQLHTNGERI NQVGITHTVN RDHIVLDVDE
     VVISHGYTSN LSDLASCGLM MSDGMVLMSQ HAETNLPGIF AAGDCATNES KVRLIAGAFN
     DAIVAVNRAK QYLNPEAAKM AYVSSHNELF RDRNRNLSRS
//
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