ID A0A1G9GMZ1_9RHOB Unreviewed; 354 AA.
AC A0A1G9GMZ1;
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:SDL02070.1};
GN ORFNames=SAMN05216257_10829 {ECO:0000313|EMBL:SDL02070.1};
OS Meinhardsimonia xiamenensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Meinhardsimonia.
OX NCBI_TaxID=990712 {ECO:0000313|EMBL:SDL02070.1, ECO:0000313|Proteomes:UP000199328};
RN [1] {ECO:0000313|Proteomes:UP000199328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10789 {ECO:0000313|Proteomes:UP000199328};
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; FNFV01000008; SDL02070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9GMZ1; -.
DR STRING; 990712.SAMN05216257_10829; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000199328; 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 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; 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 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; 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:UP000199328}.
FT DOMAIN 2..104
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 264..354
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 354 AA; 39109 MW; 512505367D93882A CRC64;
MARFLPLTVK AVEKTIRDAV VVTLEPHDPE AFRFIPGQYL TFRREIDGEE VRRSYSICSG
PDDELLQVGI KRVEGGVFST WANTELKPGD VLEAMPPMGS FHVAPAPEEA RHYLMFAGGS
GITPVLSLIR ATLAREPRAR ITLVYANRSV ATIMFREELE DLKNRHLGRL SILHILEEGQ
EVELFSGMVT EEKCAELFRL WIDVGSVDYA FICGPEPMML AIAKALRAHG LDEGRIKFEL
FASSRPAARP RPRAEGAARS ANTAEIAVTL DGTTRRFTMA KDGPSILDAA LEQDIDAPFA
CKAGVCSTCR ARVIEGEVEM VANHALEDYE VAQGYVLTCQ CHPVSDRVAV DYDQ
//
