ID A0A1H9Y427_9CLOT Unreviewed; 409 AA.
AC A0A1H9Y427;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Ferredoxin-NADP reductase {ECO:0000313|EMBL:SES63442.1};
GN ORFNames=SAMN05660297_00014 {ECO:0000313|EMBL:SES63442.1};
OS Natronincola peptidivorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Natronincola.
OX NCBI_TaxID=426128 {ECO:0000313|EMBL:SES63442.1, ECO:0000313|Proteomes:UP000199568};
RN [1] {ECO:0000313|EMBL:SES63442.1, ECO:0000313|Proteomes:UP000199568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18979 {ECO:0000313|EMBL:SES63442.1,
RC ECO:0000313|Proteomes:UP000199568};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FOHU01000001; SES63442.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9Y427; -.
DR STRING; 426128.SAMN05660297_00014; -.
DR OrthoDB; 9801223at2; -.
DR Proteomes; UP000199568; Unassembled WGS sequence.
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 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; IPR006058; 2Fe2S_fd_BS.
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:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR PRINTS; PR00371; FPNCR.
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; PS00197; 2FE2S_FER_1; 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:UP000199568}.
FT DOMAIN 55..164
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 316..407
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 409 AA; 45896 MW; 7795B13CC84AE773 CRC64;
MSKERINIKI KSLGLLDLLA FKNLVPNRKK KIQNASPTAI NEVPPMNALA LKLHPRIQHL
VIDSIKEETL STKTYRFRPD EAKGTSELAY FRSGQYLSFN FNIEGSTVTR PYSISSSPDK
TLEGCYEITV KRDEGGFVSN YIWDNWSIGT KVSCSGPEGY FYYDNLRDKR NLVALAGGCG
ITPFRSMAQS IIDGTLDINL TIFYGSNSKE DIIFYDELNA IENESNGKIH VIHVLAQEEL
EGFEKGFITK ELLEKRVNIN DSSFFICGPQ AMYNFVSGEL GKLKLRRKFV RREVFGEIKD
VESLIDFPKD VADKEFKVKV HIGGISKEIK ASAKESLLVA IERAGLCPPS SCRSGLCAIC
RSLLISGNVY IPEDDDGRRQ ADIQFGYIHP CASFPTSDLE IIIPREKKS
//
