ID B7JAZ5_ACIF2 Unreviewed; 342 AA.
AC B7JAZ5;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Ferredoxin/oxidoreductase, FAD/NAD-binding {ECO:0000313|EMBL:ACK80939.1};
GN OrderedLocusNames=AFE_1656 {ECO:0000313|EMBL:ACK80939.1};
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159 {ECO:0000313|EMBL:ACK80939.1, ECO:0000313|Proteomes:UP000001362};
RN [1] {ECO:0000313|EMBL:ACK80939.1, ECO:0000313|Proteomes:UP000001362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455
RC {ECO:0000313|Proteomes:UP000001362};
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R.II.,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
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DR EMBL; CP001219; ACK80939.1; -; Genomic_DNA.
DR RefSeq; WP_012607158.1; NC_011761.1.
DR AlphaFoldDB; B7JAZ5; -.
DR STRING; 243159.AFE_1656; -.
DR PaxDb; 243159-AFE_1656; -.
DR KEGG; afr:AFE_1656; -.
DR eggNOG; COG0633; Bacteria.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_7_0_6; -.
DR Proteomes; UP000001362; 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; cd06210; MMO_FAD_NAD_binding; 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; 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:SF5; PROTEIN RFBI; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
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:UP000001362}.
FT DOMAIN 4..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 105..208
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 342 AA; 38161 MW; 9799B7D1D52E091A CRC64;
MTNYDITIHT RDKQQVSFVC SEAEDLLSAA DRESILLPSQ CRKGTCGACV ATVTAGTYHL
GEVSMEALPE KAQARGDVLL CRTYPRADLI LEAPYDYNYI RFERIPEREA EVVDVTMVAT
GTRRLLLRLQ PDEQGGAAEF EAGQFMEIQV PGSDARRAYS LANNTNWNGD LEFFITLRPG
GAFSTYLESA LVGDRLNIRG PLGTFTLREN GLRPRWFIGG GTGLVPLLSM LRRMADWGEM
LPARLYFGAR YEDELFCQEE IRQIQDKLPQ LQVKICLSRP GNHWVDYRGS VVDALRDDLG
SLATLPDLYV CGSTRLVQGV TELALSQGLP DSCLQFERFL SA
//
