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Database: UniProt
Entry: A0A0N7JZ33_9PSEU
LinkDB: A0A0N7JZ33_9PSEU
Original site: A0A0N7JZ33_9PSEU 
ID   A0A0N7JZ33_9PSEU        Unreviewed;       399 AA.
AC   A0A0N7JZ33;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Aromatic-ring-hydroxylating dioxygenase {ECO:0000313|EMBL:ALL81140.1};
GN   ORFNames=AD017_07940 {ECO:0000313|EMBL:ALL81140.1};
OS   Pseudonocardia sp. EC080619-01.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL81140.1, ECO:0000313|Proteomes:UP000066228};
RN   [1] {ECO:0000313|EMBL:ALL81140.1, ECO:0000313|Proteomes:UP000066228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL81140.1,
RC   ECO:0000313|Proteomes:UP000066228};
RX   PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA   Van Arnam E.B., Sit C.S.;
RT   "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL   J. Am. Chem. Soc. 137:14272-14274(2015).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
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DR   EMBL; CP012184; ALL81140.1; -; Genomic_DNA.
DR   RefSeq; WP_060573792.1; NZ_CP012184.1.
DR   AlphaFoldDB; A0A0N7JZ33; -.
DR   STRING; 1096856.AD017_07940; -.
DR   KEGG; pecq:AD017_07940; -.
DR   PATRIC; fig|1096856.3.peg.1670; -.
DR   OrthoDB; 5243643at2; -.
DR   Proteomes; UP000066228; Chromosome.
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; cd08887; RHO_alpha_C_3; 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; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43756:SF5; 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   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Dioxygenase {ECO:0000313|EMBL:ALL81140.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000066228}.
FT   DOMAIN          68..175
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   399 AA;  45649 MW;  3C4150F1A20DD5E7 CRC64;
     MSTDQTAASA QQTDELAARN DRIRRALDHI RNDSTDEYDG IASFTAEEFT DPEIARRERD
     AVFGRVPSIV CHGSEIPKPN DFMTLQMPRN NVIIVRQKDH SVKAFVNLCR HRGALLEEQE
     KGRCRLFSCG YHRWSYDTDG SLRAITRDNT FGEIDRSQYG LIELPAEERH GFVWMVDDAD
     AEIDVASWLG AEMDGILAGY DMDELVSAQA EGFDEPVNWK IMQDAFLDGY HIQYAHPNTA
     AKHIHTNVMA AEDFGRHARF IAPRKTIDKY LEEPPAPDED LSPYVTETHF LLPNSTLLRQ
     PDHFELLTFR PHPTDPGRCR MEMRLVVPKV EDSGMDSERW TKIWEKNWKI LLAVLHQEDF
     PLLRSSQQGM GSANAGGMLL GRNEVINQIF HRELRKLVS
//
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