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Database: UniProt
Entry: A0A3N4RKD0_9ACTN
LinkDB: A0A3N4RKD0_9ACTN
Original site: A0A3N4RKD0_9ACTN 
ID   A0A3N4RKD0_9ACTN        Unreviewed;       358 AA.
AC   A0A3N4RKD0; A0A8G1UBJ0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Ring-1,2-phenylacetyl-CoA epoxidase subunit PaaE {ECO:0000313|EMBL:RPE28847.1};
GN   ORFNames=EDD38_5991 {ECO:0000313|EMBL:RPE28847.1}, EDD39_5887
GN   {ECO:0000313|EMBL:ROR37733.1};
OS   Kitasatospora cineracea.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=88074 {ECO:0000313|EMBL:RPE28847.1, ECO:0000313|Proteomes:UP000266906};
RN   [1] {ECO:0000313|Proteomes:UP000266906, ECO:0000313|Proteomes:UP000267408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44780 {ECO:0000313|EMBL:ROR37733.1,
RC   ECO:0000313|Proteomes:UP000267408}, and DSM 44781
RC   {ECO:0000313|EMBL:RPE28847.1, ECO:0000313|Proteomes:UP000266906};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (NOV-2018) 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:RPE28847.1}.
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DR   EMBL; RJVJ01000002; ROR37733.1; -; Genomic_DNA.
DR   EMBL; RKQG01000002; RPE28847.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4RKD0; -.
DR   Proteomes; UP000266906; Unassembled WGS sequence.
DR   Proteomes; UP000267408; 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; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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   PRINTS; PR00371; FPNCR.
DR   PRINTS; PR00410; PHEHYDRXLASE.
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}.
FT   DOMAIN          6..109
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;  38674 MW;  4203B603ACAE5CC1 CRC64;
     MAVRRPRFHP LPIGTLERLC EDAVAVTFDV PADLAEEYAF RPGQSLTLRR IVDGADERRS
     YSLCSPVGGP LRIAVREVPG GLFSHWLVGE AETGETVDVL PPSGAFTADP AVPGAHVLLA
     AGSGITPMLS IAGSVLAGHP DSTVTLLYGN RRSDTVMFAD ELADLKDRYL ERFQLVHVLS
     RETRDAELLS GRLDPERVAA LLTALVDTPA VDHWWLCGPY AMVTGAKQLL AELGVPAGRV
     HQELFHADDD EDGIVEQRHP EPEPDAAASE VTLVLDGRAS TLALPRDRAI LDGAQRARPD
     LPFACKGGVC GTCRALVCEG KVEMRRNFAL EEAELAAGYV LTCQARPVSD RVTVDYDR
//
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