ID A0A0H2M2W7_VARPD Unreviewed; 361 AA.
AC A0A0H2M2W7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=1,2-phenylacetyl-CoA epoxidase, subunit E {ECO:0000313|EMBL:KLN56774.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:KLN56774.1};
GN Name=paaE1 {ECO:0000313|EMBL:KLN56774.1};
GN ORFNames=VPARA_19770 {ECO:0000313|EMBL:KLN56774.1};
OS Variovorax paradoxus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=34073 {ECO:0000313|EMBL:KLN56774.1, ECO:0000313|Proteomes:UP000035170};
RN [1] {ECO:0000313|EMBL:KLN56774.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBEA6 {ECO:0000313|EMBL:KLN56774.1};
RA Poehlein A., Schuldes J., Wuebbeler J.H., Hiessl S., Steinbuechel A.,
RA Daniel R.;
RT "Genome sequence of Variovorax paradoxus TBEA6.";
RL Submitted (MAR-2015) 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:KLN56774.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JZWI01000009; KLN56774.1; -; Genomic_DNA.
DR RefSeq; WP_047784356.1; NZ_JZWI01000009.1.
DR AlphaFoldDB; A0A0H2M2W7; -.
DR PATRIC; fig|34073.19.peg.2029; -.
DR Proteomes; UP000035170; 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 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; IPR001589; Actinin_actin-bd_CS.
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; 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; PS00019; ACTININ_1; 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:KLN56774.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035170}.
FT DOMAIN 3..107
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 270..361
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 361 AA; 39501 MW; C23B49E1DE675776 CRC64;
MSTLFHPLRV KAVEPDTSEA VIVSFEVPPE LQQVFGFTQG QYLTLRHDID GQDLRRSYSI
CAGLDDGELR VGVRKVQGGV FSNWINAHLQ PGDTVQVMAP QGRFFVPIEP ASARHHLGIA
GGSGITPILS IMKTVLAREP LSRFTLIYGN RQLQSTMFKE EIEDLKNRYM TRLALQLVFS
DEQTDSPLGR GVMNREKIGE FLNTLVPAAS IDHAYICGPF QMNDEAEAAL LAAGVPEERI
HIERFGVALP SASQVGAVVH EALPGDAKQA RITIVRDGLQ REITFTEGQP SILDAASAAG
LEVPFSCTSG VCGTCRAKLV EGEVRMERNF ALDKNEVAAG FVLTCQAHPL TERVTLSFDE
R
//
