ID A0A0J0Y1A1_9SPHI Unreviewed; 343 AA.
AC A0A0J0Y1A1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AB669_18350 {ECO:0000313|EMBL:KLT64027.1};
OS Pedobacter sp. BMA.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1663685 {ECO:0000313|EMBL:KLT64027.1, ECO:0000313|Proteomes:UP000036014};
RN [1] {ECO:0000313|EMBL:KLT64027.1, ECO:0000313|Proteomes:UP000036014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BMA {ECO:0000313|EMBL:KLT64027.1,
RC ECO:0000313|Proteomes:UP000036014};
RA Anderson B.M., Pipes S.E., Miller J.R., Newman J.D.;
RT "Pedobacter sp. BMA.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KLT64027.1}.
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DR EMBL; LECU01000008; KLT64027.1; -; Genomic_DNA.
DR RefSeq; WP_047800819.1; NZ_LECU01000008.1.
DR AlphaFoldDB; A0A0J0Y1A1; -.
DR STRING; 1663685.AB669_18350; -.
DR PATRIC; fig|1663685.3.peg.3841; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000036014; 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; 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; 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; PR00406; CYTB5RDTASE.
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:UP000036014}.
FT DOMAIN 1..103
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 257..343
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 343 AA; 38718 MW; 500BC76F2ADB658A CRC64;
MNYTLKVAEI RKETEDTVTL CFKQPGLKKI KYIAGQYLTL IFRINGRRYI RPYSFSSCPG
VDTFLEITVK RVENGLISNH INDVVQVGDS IEVMPPMGDF IFEEGHGFKD VYFWGVGSGI
TPLLSIIKYI LSEKTEVKVH LNYGNRSHES TIFKNQIDQL KERYGDRLTI RHFHTKLVID
EANPYLIQGR IDQDKALKIL SDQSEHNGVA HYICGPAGLK ESVKNAVQAK FGNLDHVYSE
DFELVKDPKD FEDVHTQNVS LNFQGEKYTV EVVKGKSILE AALSADIELP YSCQTGNCST
CKGSMIIGEA KMIGLTKVRD DLSANEYLLC CTHPLTDNVH IEI
//
