ID B9BRP9_9BURK Unreviewed; 382 AA.
AC B9BRP9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Oxidoreductase FAD-binding domain protein {ECO:0000313|EMBL:EEE06470.1};
GN ORFNames=BURMUCGD2_4066 {ECO:0000313|EMBL:EEE06470.1};
OS Burkholderia multivorans CGD2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=513052 {ECO:0000313|EMBL:EEE06470.1, ECO:0000313|Proteomes:UP000004535};
RN [1] {ECO:0000313|EMBL:EEE06470.1, ECO:0000313|Proteomes:UP000004535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGD2 {ECO:0000313|EMBL:EEE06470.1,
RC ECO:0000313|Proteomes:UP000004535};
RX PubMed=23105085; DOI=10.1128/JB.01306-12;
RA Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., Radune D.,
RA Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., Greenberg D.E.,
RA Holland S.M., Goldberg J.B.;
RT "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic
RT Granulomatous Disease Burkholderia multivorans Isolates.";
RL J. Bacteriol. 194:6356-6357(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EEE06470.1}.
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DR EMBL; ACFC01000006; EEE06470.1; -; Genomic_DNA.
DR RefSeq; WP_006406027.1; NZ_ACFC01000006.1.
DR AlphaFoldDB; B9BRP9; -.
DR GeneID; 66528666; -.
DR Proteomes; UP000004535; 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}.
FT DOMAIN 31..134
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 298..382
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 382 AA; 42471 MW; 02B86525867B6CF4 CRC64;
MMRDAANFEP TDSRVTRPAF WNALAERWTS DVEETLVCCH VRQETHDVKS FFFRSPQGRT
FSFEPGQFIT LELDIDGETI NRCYTISSSP TRPHTISITV KRVPGGKVSN WLHDNLQPGA
SVRVLGPAGE FTCARHPARK YLFLSAGSGV TPLMSMSRAH HDLAEDRDIV FVHSARTPDD
IIFARELDLI ASNHANFRTS FVVERVGTRT NWPGVTGFLT LPLLKLIAPD FMEREIFTCG
PAPYMKAVRD LLDEAGFDRK RYHEESFSFE TLAQTASDEL LAELAPVADD AEVATKQFTV
SFAKSNREVS CGADQHVLDA ARRSGVRLPA SCTQGMCGTC KVKLVSGQVD MKHNGGIRQR
EIDQGMVLLC CSKPLSDLVI DK
//
