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Database: UniProt
Entry: E6XNC8_SHEP2
LinkDB: E6XNC8_SHEP2
Original site: E6XNC8_SHEP2 
ID   E6XNC8_SHEP2            Unreviewed;       249 AA.
AC   E6XNC8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Flavodoxin/ferredoxin--NADP reductase {ECO:0000256|ARBA:ARBA00020327};
DE            EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
DE            EC=1.19.1.1 {ECO:0000256|ARBA:ARBA00012872};
DE   AltName: Full=Ferredoxin (flavodoxin):NADP(+) oxidoreductase {ECO:0000256|ARBA:ARBA00030173};
DE   AltName: Full=Ferredoxin--NADP reductase {ECO:0000256|ARBA:ARBA00029856};
DE   AltName: Full=Flavodoxin--NADP reductase {ECO:0000256|ARBA:ARBA00030000};
GN   OrderedLocusNames=Sput200_3364 {ECO:0000313|EMBL:ADV55753.1};
OS   Shewanella putrefaciens (strain 200).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399804 {ECO:0000313|EMBL:ADV55753.1, ECO:0000313|Proteomes:UP000008209};
RN   [1] {ECO:0000313|EMBL:ADV55753.1, ECO:0000313|Proteomes:UP000008209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=200 {ECO:0000313|EMBL:ADV55753.1,
RC   ECO:0000313|Proteomes:UP000008209};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Kolker E., Lawrence C., McCue L.A., DiChristina T., Nealson K.,
RA   Fredrickson J.K., Woyke T.;
RT   "Complete sequence of Shewanella putrefaciens 200.";
RL   Submitted (JAN-2011) 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001005};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + reduced [flavodoxin] = 2 H(+) + NADPH + oxidized
CC         [flavodoxin]; Xref=Rhea:RHEA:50756, Rhea:RHEA-COMP:10622, Rhea:RHEA-
CC         COMP:10623, ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:58349; EC=1.19.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000579};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008312}.
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DR   EMBL; CP002457; ADV55753.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6XNC8; -.
DR   KEGG; shp:Sput200_3364; -.
DR   PATRIC; fig|399804.5.peg.3484; -.
DR   HOGENOM; CLU_003827_3_0_6; -.
DR   OrthoDB; 9784483at2; -.
DR   Proteomes; UP000008209; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   CDD; cd06195; FNR1; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR033892; FNR_bac.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47878:SF2; FLAVODOXIN_FERREDOXIN--NADP REDUCTASE; 1.
DR   PANTHER; PTHR47878; OXIDOREDUCTASE FAD/NAD(P)-BINDING DOMAIN PROTEIN; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          1..99
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   249 AA;  27769 MW;  C2BAAEDF614BF80E CRC64;
     MWIRGRIIER IDWNDKLFSL RIAAALTPFI PGQFIKLSQV QDEKRVARAY SLVNSPDKPY
     AEVLAVAVEE GQLSPQLQHL TIGDEIDISS TATGFMTLDE IPKGEGQGKH LWFLATGTAV
     GPFLSMLDTA EPWQRFEKIV LVYGVREAKD LAYLDKLRSY EQQYPNQFIL CLCVTREAVD
     GALQCRIPEG LASGEIEHQV GLTLSMKDSQ VMICGNPGMI SGAQSVLLDK GLTKNLRRAP
     GQITVEKYW
//
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