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Database: UniProt
Entry: A0A1I1FBL9_9GAMM
LinkDB: A0A1I1FBL9_9GAMM
Original site: A0A1I1FBL9_9GAMM 
ID   A0A1I1FBL9_9GAMM        Unreviewed;       332 AA.
AC   A0A1I1FBL9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Ferredoxin-NADP reductase {ECO:0000313|EMBL:SFB96372.1};
GN   ORFNames=SAMN02745724_00564 {ECO:0000313|EMBL:SFB96372.1};
OS   Pseudoalteromonas denitrificans DSM 6059.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1123010 {ECO:0000313|EMBL:SFB96372.1, ECO:0000313|Proteomes:UP000198862};
RN   [1] {ECO:0000313|EMBL:SFB96372.1, ECO:0000313|Proteomes:UP000198862}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6059 {ECO:0000313|EMBL:SFB96372.1,
RC   ECO:0000313|Proteomes:UP000198862};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004533}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}.
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DR   EMBL; FOLO01000003; SFB96372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1FBL9; -.
DR   STRING; 1123010.SAMN02745724_00564; -.
DR   OrthoDB; 9784483at2; -.
DR   Proteomes; UP000198862; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   CDD; cd06194; FNR_N-term_Iron_sulfur_binding; 1.
DR   Gene3D; 3.10.20.30; -; 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; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
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; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198862};
KW   Ubiquinone {ECO:0000256|ARBA:ARBA00023075}.
FT   DOMAIN          2..87
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          88..188
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   332 AA;  37470 MW;  C9059F38D9ABEB82 CRC64;
     MPNIYFNSQK IPFKVGQSIL DALIEFDFKP VYSCKKGVCQ TCMLKSDSSQ ITQSQMEVKD
     TLKVQGYFLP CQCYPDSDIS VISPCSEDIT YDMQVSDKKL LTQDIVQLKL VFTSDNRVFI
     RAGQFINLKV QNDILRSYSV ANTPEKDGYI ELHIQKVPDG KMSAWCFEHA NIGSALSMIG
     PFGKCIYLSD FKNDDLVLIG TGTGLAPLIG IINQALSNKH KGKITLFHGS RHFNGLYLHQ
     TLKKLADTHE NFYYKPCLSG EIPQTLADEN INNGRVNKVA MMQLNKQKGD YKNIRFYLCG
     HPEMVKNMQK MAYLSGAILS KINADPFEYT AY
//
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