ID A0A1Q4D6F4_9PSEU Unreviewed; 419 AA.
AC A0A1Q4D6F4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=p-cumate dioxygenase {ECO:0000313|EMBL:OJY39848.1};
GN ORFNames=BGP03_21450 {ECO:0000313|EMBL:OJY39848.1};
OS Pseudonocardia sp. 73-21.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1895809 {ECO:0000313|EMBL:OJY39848.1, ECO:0000313|Proteomes:UP000186163};
RN [1] {ECO:0000313|EMBL:OJY39848.1, ECO:0000313|Proteomes:UP000186163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73-21 {ECO:0000313|EMBL:OJY39848.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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:OJY39848.1}.
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DR EMBL; MKVV01000091; OJY39848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4D6F4; -.
DR STRING; 1895809.BGP03_21450; -.
DR Proteomes; UP000186163; 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:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR CDD; cd08879; RHO_alpha_C_AntDO-like; 1.
DR CDD; cd03469; Rieske_RO_Alpha_N; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756:SF1; 3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:OJY39848.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 47..156
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 419 AA; 46971 MW; 0519829B4E23FB22 CRC64;
MTVTDARTDA YVDDDRAHHR FRVHRSTMTS PDVFALEIER IFGRCWLYVG HESEIRERGD
YVRRPIANRQ VFMVRSRSGQ VKVFHNTCPH RGATICRKDA GNAKVFQCFY HAWSFDTEGS
LVGVPDREAY GDGLDFSALG LRSVARVESY RGFVFACFDP DVVGLVEYLA GAAEYLDLIV
DATGDAEIIS GTNAYAIDAN WKLLAENSID GYHAVPTHDT YFKYLTALGT SLAGGVAGTA
TGLGNGHAVL EYRAPWGRPV AKWEPLFGED AREEIDRLRA DLVGRHGEER AARMADTNRN
LLIYPNLVVN DIMAITVRTF MPVSAERMEV TAWELAPRDE LPELRQRRLD SFLTFLGPGG
FATPDDIEAL ESCQQGFRSG GVEWNDISRG MARDVPQTND EEQMRAFWRQ WASHMAGDL
//
