ID A0A238VPM7_9FLAO Unreviewed; 357 AA.
AC A0A238VPM7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Ring-1,2-phenylacetyl-CoA epoxidase subunit PaaE {ECO:0000313|EMBL:SNR36168.1};
GN ORFNames=SAMN06265376_101147 {ECO:0000313|EMBL:SNR36168.1};
OS Dokdonia pacifica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Dokdonia.
OX NCBI_TaxID=1627892 {ECO:0000313|EMBL:SNR36168.1, ECO:0000313|Proteomes:UP000198379};
RN [1] {ECO:0000313|EMBL:SNR36168.1, ECO:0000313|Proteomes:UP000198379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25597 {ECO:0000313|EMBL:SNR36168.1,
RC ECO:0000313|Proteomes:UP000198379};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FZNY01000001; SNR36168.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238VPM7; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000198379; 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:UP000198379}.
FT DOMAIN 2..106
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 267..357
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 357 AA; 39912 MW; B05B72AD7E0D7E21 CRC64;
MAQFHNITIK DIYKETSDCS VVTFDIPEAL HSAFDFQQGQ HLTLKAILDG QDVRRSYSLC
SSPVDKEWKV AVKQIPGGLF SSYVNEKLKA GDILEVMEPS GKFGVPVSKD SAKNYVVFAA
GSGITPILSM IKTHLALEPN AKFKLFYLNR TVKSIIFKEE IEQLRNQYFG RLEIFYFLTK
EQRDIELFNG RFTSDKLQTL TKTLISVEAT DEVFICGPEE MIFLIRDELV TAGLEKDKVH
YELFVTGLSE EDKQRAARLA EQQVEGVEVT IVDGGKDFHF TMTDEYDNIL DAALGAGADL
PFACKGGVCS TCKCKVEEGS VEMKINYALE ENEVAQNLVL SCQAVPTSEN VKVNFDV
//
