ID A0A150AEN9_9BACT Unreviewed; 343 AA.
AC A0A150AEN9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AVL50_21625 {ECO:0000313|EMBL:KXX68370.1};
OS Flammeovirga sp. SJP92.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC Flammeovirga.
OX NCBI_TaxID=1775430 {ECO:0000313|EMBL:KXX68370.1, ECO:0000313|Proteomes:UP000075267};
RN [1] {ECO:0000313|EMBL:KXX68370.1, ECO:0000313|Proteomes:UP000075267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJP92 {ECO:0000313|EMBL:KXX68370.1,
RC ECO:0000313|Proteomes:UP000075267};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-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:KXX68370.1}.
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DR EMBL; LQAQ01000093; KXX68370.1; -; Genomic_DNA.
DR RefSeq; WP_062618630.1; NZ_LQAQ01000093.1.
DR AlphaFoldDB; A0A150AEN9; -.
DR STRING; 1775430.AVL50_21625; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000075267; 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; 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; PR00406; CYTB5RDTASE.
DR PRINTS; PR00371; FPNCR.
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:UP000075267}.
FT DOMAIN 1..104
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 255..343
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 343 AA; 37778 MW; CD4100A3E28F88FE CRC64;
MNQITLKVKE VVHETSDTVT IKLKQPLFKK VQYQAGQFLT IIAEVGGQKL RRSYSMSSAP
HLDATIDITV KRIPDGKVSN HLNDNVKAGD MLEVVEPMGQ FVYEPDKDTE RHVVLWGAGS
GITPLFSMLK SCLFFEPKSK VTLVFGNRNE ESVIFKKSLE ELKEKFEDRL EVVHVMSRPS
AQWGGFSGRI DDVVAINIMN RLSLDHSEHY LCGPDGMMDA VSNALKRNKM ASSKIFKESF
TPVSGSDHSD NVSSENILLV VDGEEHSVFV APDQTILEAA LEEGLDVPYS CQNGVCTACR
ANCSSGKVEM GDTSVLSQSE MDNGDILTCI SHPLGGNVKI TYD
//