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Database: UniProt
Entry: A0A1H9B845_9PSEU
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ID   A0A1H9B845_9PSEU        Unreviewed;       351 AA.
AC   A0A1H9B845;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Ring-1,2-phenylacetyl-CoA epoxidase subunit PaaE {ECO:0000313|EMBL:SEP84907.1};
GN   ORFNames=SAMN05216188_101678 {ECO:0000313|EMBL:SEP84907.1};
OS   Lentzea xinjiangensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=402600 {ECO:0000313|EMBL:SEP84907.1, ECO:0000313|Proteomes:UP000199352};
RN   [1] {ECO:0000313|Proteomes:UP000199352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3525 {ECO:0000313|Proteomes:UP000199352};
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; FOFR01000001; SEP84907.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9B845; -.
DR   STRING; 402600.SAMN05216188_101678; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000199352; 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   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          10..109
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          262..351
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   351 AA;  37565 MW;  7A5F7255A57D3FFB CRC64;
     MPPAPGKRGA AFHKLTVARV DRLCDDAVAV TFDVPADLAD EFAFSAGQYL TVRQGDERRS
     YSICAPAGAA PRIGVRRVDG GQFSTWLVDR VAPGDVLEVL PPLGKFSPTG VGTHHGFVVA
     GSGITPALSI AATVLATGAR VTLLYGNRST NTVMFADELA DLKDRYPATF QLIHVLSREP
     RDVELFTGRL TAAKLTALFG TVVPFDAIDE WWLCGPYEMV QDATAVLRDR GVPTDRVHHE
     LFYVDEPPPP PRRAEAVVDS AATVTVVLDG KSTTLPLPTG EPVLDAAQRV RADLPFACKG
     GVCGTCRALV TEGSVEMRRN YALDESEVAA GFVLTCQALP TSERVTVDFD A
//
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