ID A0A1I2KJC2_9GAMM Unreviewed; 319 AA.
AC A0A1I2KJC2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Ring-1,2-phenylacetyl-CoA epoxidase subunit PaaE {ECO:0000313|EMBL:SFF66340.1};
GN ORFNames=SAMN04488120_1203 {ECO:0000313|EMBL:SFF66340.1};
OS Fontimonas thermophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Fontimonas.
OX NCBI_TaxID=1076937 {ECO:0000313|EMBL:SFF66340.1, ECO:0000313|Proteomes:UP000199771};
RN [1] {ECO:0000313|EMBL:SFF66340.1, ECO:0000313|Proteomes:UP000199771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23609 {ECO:0000313|EMBL:SFF66340.1,
RC ECO:0000313|Proteomes:UP000199771};
RA de Groot N.N.;
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};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
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DR EMBL; FOOC01000020; SFF66340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2KJC2; -.
DR STRING; 1076937.SAMN04488120_1203; -.
DR Proteomes; UP000199771; 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 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; 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; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF6; 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; 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:UP000199771}.
FT DOMAIN 1..83
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 229..319
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 319 AA; 34533 MW; C12540ABCDCDED4A CRC64;
MVLAPEDGIP HGVRAGQFLT LIAQIDGRTV KRAYSLSELP KDGTLTITSK RVAGGVMSMY
LNARLRAGDW IQFAGPSGDF VLPARTPDYY VFAAAGSGIT PIMAMLEQLL DHEHSRRPIT
VVYGNRREQD ILFRSRLDAW ADRHENLSIR YWLSKPAKGW SGGVGRIDAG ALLDAAPGSA
AFYFLCGPGN FNTAVRSELI ARGVPAQAIV SEQFTTLARE SRPHPKDPHP VLFRVGGSEK
EVTVRPGETL LEAGLRAGVA LPFSCTMGGC GHCKIKVLDG DVATDTPNCL TELERQAGYA
LACCAYPHRR ATVTVEEKV
//