ID C6KTX9_9BACT Unreviewed; 368 AA.
AC C6KTX9;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Ferredoxin oxidoreductase {ECO:0000313|EMBL:BAH89430.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:BAH89430.1};
RN [1] {ECO:0000313|EMBL:BAH89430.1}
RP NUCLEOTIDE SEQUENCE.
RA Suenaga H., Ohnuki T., Miyazaki K.;
RT "Functional screening of a metagenomic library for genes involved in
RT microbial degradation of aromatic compounds.";
RL Environ. Microbiol. 9:2289-2297(2007).
RN [2] {ECO:0000313|EMBL:BAH89430.1}
RP NUCLEOTIDE SEQUENCE.
RA Suenaga H., Koyama Y., Miyakoshi M., Miyazaki R., Yano H., Sota M.,
RA Ohtsubo Y., Tsuda M., Miyazaki K.;
RT "Novel organization of aromatic degradation pathway genes in a microbial
RT community as revealed by metagenomic analysis.";
RL ISME J. 0:0-0(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; AB266116; BAH89430.1; -; Genomic_DNA.
DR AlphaFoldDB; C6KTX9; -.
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; cd06214; PA_degradation_oxidoreductase_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; 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:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR PANTHER; PTHR47354; 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 32..137
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 279..368
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 368 AA; 39459 MW; 178B268F0E4A228E CRC64;
MTIGYCNFIL HAILEEIVTL VQAIPASGET ASGFTRLRVK AVIAETADAS SIVFETPDEQ
ANAFRYKPGQ FLTLRVPVNG EDELRCYSLA SSPATGENLK VTVKRVADGR VSNWLLDNLG
AGDNLLVMPP KGIFCLQEGV GSVVLFAAGS GITPVISILK QVLLTTARKV KLVYANRDRN
SIIFREELER LRDFHKGRFE LVHRLDTEQG ILTAQDAGAH ADPAGQHYLC GPAPFMQAVK
DGLRAAGVPD ARILMESFDL AEDEPATEAA PVSDGANVAK VTVRYRGADY AIEVLETETV
HTAAKRQGLN LPFSCKAGFC GLCIARVTAG QVSLKDNLGA ISDGQIAEGL TLTCQALVRS
AEATVVFE
//
