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Database: UniProt
Entry: A0A150AEN9_9BACT
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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
//
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