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Database: UniProt
Entry: A0A1I5RLL0_9ACTN
LinkDB: A0A1I5RLL0_9ACTN
Original site: A0A1I5RLL0_9ACTN 
ID   A0A1I5RLL0_9ACTN        Unreviewed;       358 AA.
AC   A0A1I5RLL0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Ring-1,2-phenylacetyl-CoA epoxidase subunit PaaE {ECO:0000313|EMBL:SFP59425.1};
GN   ORFNames=SAMN05660464_3607 {ECO:0000313|EMBL:SFP59425.1};
OS   Geodermatophilus dictyosporus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1523247 {ECO:0000313|EMBL:SFP59425.1, ECO:0000313|Proteomes:UP000198857};
RN   [1] {ECO:0000313|Proteomes:UP000198857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44208 {ECO:0000313|Proteomes:UP000198857};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FOWQ01000006; SFP59425.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5RLL0; -.
DR   STRING; 1523247.SAMN05660464_3607; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000198857; 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   GO; GO:0010124; P:phenylacetate catabolic process; 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; IPR011884; PaaE.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   NCBIfam; TIGR02160; PA_CoA_Oxy5; 1.
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   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:UP000198857}.
FT   DOMAIN          9..112
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          269..358
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   358 AA;  38895 MW;  A638742BE65FC918 CRC64;
     MSAPARRRPR FHPLRVASVE RLTDDAVAVT FDVPPELAED YAFRPGQALT LRRVDGDRDE
     RRSYSICAPV GAPPRVGVRE VPGGFFSSWL VHEVAPGDEI EVLPPSGTFT ADLSQPGDHV
     FVVAGSGITP ALSLAGTVLR DGESTVTVFY GNRRTNTVMF ADELADLKDR YGPRLQLVHV
     LSREPRDAEV TTGRLDGDRL RTLVGAFVDA GHVDHWWLCG PHGMVSDARE LLAGLGVPAE
     RVHQELFYVD DVPPQPVRGD DETVEGPSSQ VTVVLDGRST TLALPRDVPV LDSAQRVRSD
     LPFACKGGVC GTCRARVTDG EVEMRRNYAL EAEEVEAGYV LTCQTLPLSD AVTVDFDA
//
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