ID A0A0G3EPK0_9BURK Unreviewed; 329 AA.
AC A0A0G3EPK0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Ferredoxin {ECO:0008006|Google:ProtNLM};
GN ORFNames=ABW99_06550 {ECO:0000313|EMBL:AKJ67929.1};
OS Pandoraea thiooxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pandoraea.
OX NCBI_TaxID=445709 {ECO:0000313|EMBL:AKJ67929.1, ECO:0000313|Proteomes:UP000036700};
RN [1] {ECO:0000313|Proteomes:UP000036700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25325 {ECO:0000313|Proteomes:UP000036700};
RA Lim Y.L., Ee R., Yong D., How K.Y., Yin W.F., Chan K.G.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP011568; AKJ67929.1; -; Genomic_DNA.
DR RefSeq; WP_047213749.1; NZ_CP014839.1.
DR AlphaFoldDB; A0A0G3EPK0; -.
DR STRING; 445709.ABW99_06550; -.
DR KEGG; ptx:ABW99_06550; -.
DR PATRIC; fig|445709.3.peg.1404; -.
DR OrthoDB; 544091at2; -.
DR Proteomes; UP000036700; Chromosome.
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; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF2; PHENOXYBENZOATE DIOXYGENASE BETA SUBUNIT; 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 Reference proteome {ECO:0000313|Proteomes:UP000036700}.
FT DOMAIN 6..117
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 244..329
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 329 AA; 35400 MW; 1F9D9B3503FA9373 CRC64;
MTTNPENPLE LRVDRVRALS PQITAFELRA ADGAALPGFT PGAHVQVEVA PGGVPQWRHY
SLVNFDTAAH VTQAPGTYLI AVRREDQGRG GSSWLHANVR AGDILRVRPP HNDFALTDCH
DAVLIAGGIG ITPLASMTAA LVADGHNFAL HYSGRSIAQL AFTAELRALA AHRLHLYGDD
DPAHRLDLAR LLATLRPTQP LYVCGPKGMI DAAIGQACAL GWAREDVHVE LFTAAEPQAG
DTGFEVELRQ SGVVLSVRPE QTILDAMLDA GLDPLYDCKR GECGVCQTSV LEGAVEHRDY
CLSEREKQSG QVMQICVSRA RGARLVLDA
//
