ID A0A1W9I4B5_9PROT Unreviewed; 316 AA.
AC A0A1W9I4B5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:OQW54311.1};
GN ORFNames=A4S14_15135 {ECO:0000313|EMBL:OQW54311.1};
OS Proteobacteria bacterium SG_bin9.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1827385 {ECO:0000313|EMBL:OQW54311.1, ECO:0000313|Proteomes:UP000192684};
RN [1] {ECO:0000313|EMBL:OQW54311.1, ECO:0000313|Proteomes:UP000192684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG_bin9 {ECO:0000313|EMBL:OQW54311.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
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:OQW54311.1}.
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DR EMBL; LWDM01000073; OQW54311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9I4B5; -.
DR STRING; 1827385.A4S14_15135; -.
DR Proteomes; UP000192684; 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; cd06185; PDR_like; 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; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
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 3..105
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 229..316
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 316 AA; 34587 MW; 08F9AB930DE265B8 CRC64;
MVLDELKLRV TARSLAADGV VLIELQPADG EILPGFKPGA HIEVQLPDGL RRHYSLCGDP
DARDRYRIAV ALAEPSRGGS AYMHQSLNVG DVIVTSTPRN NFPLVEDSQR YQFIAGGIGI
TPILPMLRWC EANNRSWRLL YLLRGRARAA FLDDLAPFAG RVQTHFDDEA GGVFDIGAAL
NDVARDAHIY CCGPGPLMEA VEQAAADRDS AYVHFEWFTP KDQSALANTP FTVILARSRR
EVAIPADRSI LETLQASGMK LPFSCREGLC ATCETAVLAG TPDHRDQILT PEEKQVSQSM
MICVSRAKSP SITLDL
//
