ID A0A3E1NLT2_9BACT Unreviewed; 345 AA.
AC A0A3E1NLT2;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Ring-1,2-phenylacetyl-CoA epoxidase subunit PaaE {ECO:0008006|Google:ProtNLM};
GN ORFNames=DXN05_09030 {ECO:0000313|EMBL:RFM28900.1};
OS Deminuibacter soli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Deminuibacter.
OX NCBI_TaxID=2291815 {ECO:0000313|EMBL:RFM28900.1, ECO:0000313|Proteomes:UP000261284};
RN [1] {ECO:0000313|EMBL:RFM28900.1, ECO:0000313|Proteomes:UP000261284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K23C18032701 {ECO:0000313|EMBL:RFM28900.1,
RC ECO:0000313|Proteomes:UP000261284};
RA Wang C.;
RT "Chitinophagaceae sp. K23C18032701, a novel bacterium isolated from forest
RT soil.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RFM28900.1}.
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DR EMBL; QTJU01000002; RFM28900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E1NLT2; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000261284; 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; 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; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
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:UP000261284}.
FT DOMAIN 1..104
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 258..345
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 345 AA; 38472 MW; 7734315D3E729015 CRC64;
MTYQRLQITA IHEETPVCKT FELQPLDKWE PQYTAGQFLT LVFSKNGTER RRSYSFSSAP
LLGEPMRITI KRVVNGEYSR QLLDHSKTGD ILTTAGISGL FQLPEGTALQ QTQQLFFLAA
GSGIVPVFAL LKTALHTTQL PVILVFSNRS AADAIFYNEL QLLQQTFAGR LHIEFLFSDI
AHVRKSRLSN WLLLQLLQEL VTVPITKCLF YMCGPFEYMQ TIGITLLAEG VPALHIRKEN
FSSIPPAKKP APPDTGAHKA TIHLHHHTHE VMVQYPHSIL AAAKAKGIEL PYSCEAGRCG
SCIATCTSGK IWMAYNEILV NEEIAQGRIL TCQSFPVDGD VEIKF
//
