ID C0KUL0_9MYCO Unreviewed; 488 AA.
AC C0KUL0;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Phthalate dioxygenase large subunit {ECO:0000313|EMBL:ACN38276.1};
GN Name=phtAa {ECO:0000313|EMBL:ACN38276.1};
OS Mycobacterium sp. CH1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=597355 {ECO:0000313|EMBL:ACN38276.1};
RN [1] {ECO:0000313|EMBL:ACN38276.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CH1 {ECO:0000313|EMBL:ACN38276.1};
RA Churchill P.F., Kitchens E.J.;
RT "pht operon for phthalate degradation.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; FJ641978; ACN38276.1; -; Genomic_DNA.
DR AlphaFoldDB; C0KUL0; -.
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 GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08881; RHO_alpha_C_NDO-like; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR043266; RHO_NdoB-like_C.
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 Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:ACN38276.1};
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 43..156
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT REGION 468..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 54558 MW; 7A3396F1BCA0715D CRC64;
MELNMQDHGE VLAAVRTGMI PAHVYNDKRI FSLEKERLFS RAWLFVAHES EIPQPGDYVV
RQVLQDSFIV ARDSAGEIRV MFNMCLHRGM QVCRAEMGNA SNFRCPYHGW SYRNDGRIIG
LPFHQEAYGG DAGFNKAGQT LLPAPSVASY NGLIFLSMDP DAESLEEYLG DFRFYLDFYT
KQGPNGLEVR GPQRWRVKAN WKIAAENFAG DMYHTPQTHT SVVEIGLFRE PKANKRKDGA
TYWAGRGGGT TYKLPEGSFE DRMSYVGYPA EMISRAKATW TEQQQQVVGT DGFMISAATC
FPNISFVHNW PKVEDGEHVL PFISIRVWQP ISENETEVLS WFAVDSDAPA DFKADSYKAY
LMCFGSTGMF EQDDVENWVS LTNTAGGSMA RRLRLNSRMG LLADDVRVVD TLSSAQFHGP
GYAQLGYNEN NQRQLLRLWA DYLDMPPLRV DPATVLSDNP HGIEPMVQTN GAGAAGIDSG
SAPTSVML
//
