ID A0A0P1IBQ5_9RHOB Unreviewed; 358 AA.
AC A0A0P1IBQ5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=1,2-phenylacetyl-CoA epoxidase, subunit E {ECO:0000313|EMBL:CUK03819.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:CUK03819.1};
GN Name=paaE {ECO:0000313|EMBL:CUK03819.1};
GN ORFNames=PH7735_02706 {ECO:0000313|EMBL:CUK03819.1};
OS Shimia thalassica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1715693 {ECO:0000313|EMBL:CUK03819.1, ECO:0000313|Proteomes:UP000051870};
RN [1] {ECO:0000313|Proteomes:UP000051870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7735 {ECO:0000313|Proteomes:UP000051870};
RA Rodrigo-Torres Lidia, Arahal R.David.;
RL Submitted (SEP-2015) 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; CYTW01000003; CUK03819.1; -; Genomic_DNA.
DR RefSeq; WP_058311896.1; NZ_CYTW01000003.1.
DR AlphaFoldDB; A0A0P1IBQ5; -.
DR STRING; 1715693.PH7735_02706; -.
DR GeneID; 83881715; -.
DR Proteomes; UP000051870; 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:UniProtKB-KW.
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; 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 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 Oxidoreductase {ECO:0000313|EMBL:CUK03819.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051870}.
FT DOMAIN 2..106
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; 38709 MW; 95A17D206C96B950 CRC64;
MARFHDLEVT DIQKTIRDAV VVTLKPVNGA AEAFDFTQGQ YLTFRQDFDG DELRRSYSIC
AGKDDGILQV GIKRVDGGTF STWANEDLKI GDTVQAMPPM GGFFTALDAG NEKNYLGFAG
GSGITPVLSI LKTTLAAEPN STFTLVYANK GVNTIMFREE LEDLKNTYMG RFNVIHILET
DAQEIDLFTG LVTEDKCAQL FATGWIDIGS VDTAFICGPE PMMLGIAAAL RTGGLTDAQI
KFELFASSQP GRAKRKAVSK NAASGANQAS ATITLDGSTQ AIEMPKDTTI LDAALDNKMD
APFACKAGVC STCRCRVLEG EVEMVSNHAL EDYEVEKGYV LSCQSYPVTD NVVVDFDQ
//
