ID A0A0P0SL65_9PSEU Unreviewed; 323 AA.
AC A0A0P0SL65;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:ALL85473.1};
GN ORFNames=AD017_30560 {ECO:0000313|EMBL:ALL85473.1};
OS Pseudonocardia sp. EC080619-01.
OG Plasmid pBCI1-2 {ECO:0000313|EMBL:ALL85473.1,
OG ECO:0000313|Proteomes:UP000066228}.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL85473.1, ECO:0000313|Proteomes:UP000066228};
RN [1] {ECO:0000313|EMBL:ALL85473.1, ECO:0000313|Proteomes:UP000066228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL85473.1,
RC ECO:0000313|Proteomes:UP000066228};
RC PLASMID=Plasmid pBCI1-2 {ECO:0000313|Proteomes:UP000066228};
RX PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA Van Arnam E.B., Sit C.S.;
RT "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL J. Am. Chem. Soc. 137:14272-14274(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP012185; ALL85473.1; -; Genomic_DNA.
DR RefSeq; WP_060577165.1; NZ_CP012185.1.
DR AlphaFoldDB; A0A0P0SL65; -.
DR KEGG; pecq:AD017_30560; -.
DR PATRIC; fig|1096856.3.peg.6767; -.
DR OrthoDB; 3807506at2; -.
DR Proteomes; UP000066228; Plasmid pBCI1-2.
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; IPR001433; OxRdtase_FAD/NAD-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 Pfam; PF00175; NAD_binding_1; 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};
KW Plasmid {ECO:0000313|EMBL:ALL85473.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000066228}.
FT DOMAIN 7..109
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 238..323
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 323 AA; 34853 MW; DBD449C735477F1D CRC64;
MRTDVHDDEL DLVLDKKETV ADGVVRLTLR STDGAELPVW EAGAHLDLVL TDELTRQYSL
CGDPAERSIL QVAALREPDG RGGSAYVHDT LAEGDTVHVR GPRNHFPLTP AGRYVFVAGG
IGITPLLPMI ARAEAAGADW RLVYGGRTRT SMAFREHLEQ SYPDRVEIRP ADETGLLDLP
TILAEPGATA DDIAVYCCGP EPLLAAVEQE CTRWPRGALH LERFAPKAGT DDGPRESFEV
ELSQSRATLT VPADRSILEV VENAGIPVLS SCQEGTCGTC ETGVLDGVPD HRDSVLSDDE
QADGDVMMIC VSRSCSARLV LDL
//
