ID A0A0W7X7H1_9ACTN Unreviewed; 303 AA.
AC A0A0W7X7H1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Phthalate 4,5-dioxygenase {ECO:0000313|EMBL:KUF18705.1};
GN ORFNames=AT728_06515 {ECO:0000313|EMBL:KUF18705.1};
OS Streptomyces silvensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1765722 {ECO:0000313|EMBL:KUF18705.1, ECO:0000313|Proteomes:UP000054804};
RN [1] {ECO:0000313|EMBL:KUF18705.1, ECO:0000313|Proteomes:UP000054804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53525 {ECO:0000313|EMBL:KUF18705.1,
RC ECO:0000313|Proteomes:UP000054804};
RA Johnston C.W., Li Y., Magarvey N.A.;
RT "Draft genome sequence of Streptomyces silvensis ATCC 53525, a producer of
RT novel hormone antagonists.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KUF18705.1}.
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DR EMBL; LOCL01000029; KUF18705.1; -; Genomic_DNA.
DR RefSeq; WP_058846864.1; NZ_LOCL01000029.1.
DR AlphaFoldDB; A0A0W7X7H1; -.
DR STRING; 1765722.AT728_06515; -.
DR OrthoDB; 502624at2; -.
DR Proteomes; UP000054804; 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; 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; 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:KUF18705.1};
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:KUF18705.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054804}.
FT DOMAIN 1..101
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 214..303
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 303 AA; 32401 MW; 4B80D22A53A80370 CRC64;
MQQHTVIDRA EDIAEGVVSL LLRGTTGSLA PWEPGAHIDL SLPNWLTRSY SLCGDPADAE
HYRVAVRHDP LSRGGSEYIH HYLRAGRALK VSLPRNHFPL LPAPRYLFLA GGIGITPLLP
MLAAAVEADV PATLVYAGRS AAAMPFAEEL RSRHGDRVRL VATREDGRPD LTALAAGLAP
DTLVYCCGPA PMIAAAQAAF PADRLHTERF RPAPRVFAEN KPFDAVCARS GRTVPVPADQ
SLLDALNRAG IPVAAGCREG VCGSCELTVL SGTPEHRDDI GASDGRVYAC VTRALTPELV
IDR
//
