ID A0A1Q8J0I5_9BURK Unreviewed; 321 AA.
AC A0A1Q8J0I5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Phthalate 4,5-dioxygenase {ECO:0000313|EMBL:OLL32452.1};
GN ORFNames=BTH42_08435 {ECO:0000313|EMBL:OLL32452.1};
OS Burkholderia sp. SRS-W-2-2016.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1926878 {ECO:0000313|EMBL:OLL32452.1, ECO:0000313|Proteomes:UP000186182};
RN [1] {ECO:0000313|Proteomes:UP000186182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRS-W-2-2016 {ECO:0000313|Proteomes:UP000186182};
RA Chauhan A.;
RL Submitted (DEC-2016) 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:OLL32452.1}.
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DR EMBL; MSDV01000019; OLL32452.1; -; Genomic_DNA.
DR RefSeq; WP_075297790.1; NZ_MSDV01000019.1.
DR AlphaFoldDB; A0A1Q8J0I5; -.
DR STRING; 1926878.BTH42_08435; -.
DR OrthoDB; 544091at2; -.
DR Proteomes; UP000186182; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06185; PDR_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; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 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; PR00409; PHDIOXRDTASE.
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 Dioxygenase {ECO:0000313|EMBL:OLL32452.1};
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:OLL32452.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186182}.
FT DOMAIN 6..108
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 238..321
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 321 AA; 35712 MW; D2A8C6B603D9CD40 CRC64;
MTPQEDLFLR VRIERKEKIA RDIWRFELTS ADGGTVPSFE AGSNLTVQIP NGMRRSYSLC
NDPNENHRYV IAVKREGNGR GGSISLVDET SEGDMLDVSP PRNDFPLDGR AREFILVAGG
IGITPMLSMA RQLKSEEGLR KFRLIYLARD PEGTAFIDEL QSGEWRSFVK IHHDFGDPGR
SFDFWSLFER PKQAHVYCCG PNALMDTVKD MTGHWPSGTV HFESFGAANV AARENRPFTI
RLQRSGTTLD VPANRSILDV LRSANVRVAS SCESGTCGSC KTGLCAGEAD HRDLVLQDGE
RETQIMVCVS RAKSQELVLD L
//
