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Database: UniProt
Entry: A0A1I2KJC2_9GAMM
LinkDB: A0A1I2KJC2_9GAMM
Original site: A0A1I2KJC2_9GAMM 
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
//
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