ID A0A1N6IHJ5_9BURK Unreviewed; 380 AA.
AC A0A1N6IHJ5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Ferredoxin-NADP reductase {ECO:0000313|EMBL:SIO31496.1};
GN ORFNames=SAMN05444165_2177 {ECO:0000313|EMBL:SIO31496.1};
OS Paraburkholderia phenazinium.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=60549 {ECO:0000313|EMBL:SIO31496.1, ECO:0000313|Proteomes:UP000185151};
RN [1] {ECO:0000313|EMBL:SIO31496.1, ECO:0000313|Proteomes:UP000185151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS95 {ECO:0000313|EMBL:SIO31496.1,
RC ECO:0000313|Proteomes:UP000185151};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FSRU01000001; SIO31496.1; -; Genomic_DNA.
DR RefSeq; WP_074295662.1; NZ_FSRU01000001.1.
DR AlphaFoldDB; A0A1N6IHJ5; -.
DR OrthoDB; 370747at2; -.
DR Proteomes; UP000185151; 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 CDD; cd06215; FNR_iron_sulfur_binding_1; 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; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF6; 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; 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; 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:UP000185151}.
FT DOMAIN 31..134
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 296..380
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 380 AA; 42249 MW; 313F587FEDF79501 CRC64;
MMRDAATFEP VESRLTKPQF WGTLPARWTS DVEETLVCCQ VRQETHDVKS FFFRSPAGHG
FSFEPGQFVT LELEIDGETI NRCYTISSSP TRPHTISITV KRVPGGKVSN WLHDNLQAGA
QVRVLGPSGE FTCARHPARK YLFLSAGSGI TPLMSMSRAH HELSEDRDIA FVHSARTPED
IIFARELDLI ATNQSNFRAS FVCERVGTRT NWPGVTGFLT LPLLKLIAPD FMEREVFTCG
PAPYMKAVRD LLDEAGFDRR HYHEESFSFE TLIEEAPELL AEVAPAENGD VLANTFAVSF
SRSNREIHCG TDQHVLDAAR QAGVRLPASC TQGMCGTCKV KLVSGQVEMK HNGGIRQREI
DQGMVLLCCS KPLSDLVVDK
//
