ID C1BB28_RHOOB Unreviewed; 437 AA.
AC C1BB28;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=p-cumate dioxygenase large subunit {ECO:0000313|EMBL:BAH52881.1};
GN Name=cmtA1 {ECO:0000313|EMBL:BAH52881.1};
GN Synonyms=cmtAb {ECO:0000313|EMBL:BAH52881.1};
GN OrderedLocusNames=ROP_46340 {ECO:0000313|EMBL:BAH52881.1};
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH52881.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH52881.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH52881.1,
RC ECO:0000313|Proteomes:UP000002212};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-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; AP011115; BAH52881.1; -; Genomic_DNA.
DR RefSeq; WP_012691799.1; NC_012522.1.
DR AlphaFoldDB; C1BB28; -.
DR STRING; 632772.ROP_46340; -.
DR KEGG; rop:ROP_46340; -.
DR PATRIC; fig|632772.20.peg.4846; -.
DR HOGENOM; CLU_026244_4_0_11; -.
DR OrthoDB; 5243643at2; -.
DR Proteomes; UP000002212; 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; 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:BAH52881.1};
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 41..139
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 437 AA; 48620 MW; D0D2C97EF1F0C4D8 CRC64;
MTAEQFIIDD RENNLFRVNR EAFTSEDVLQ RERKEIFGKT WLYVGHESEI PGKNDFQTRD
VGGRPVIFNR DRHGDVRVLL NTCLHRGSSV CRHSSGNAKI FTCFYHGWAY RNSGELVNVP
GNEDYKSEPA AVYKGLQSPA QVDSYRGLYF VNFDPDAPDL LTFLGEARYF IDLAADQSPE
GVAILEGTHK YSLKANWKLL VENSIDGYHA KSVHHTHFEM MMELGATPPM LGKDTVNGIA
PAGMGTEFPN GHATLMYPAN GLPLATDSVK QTLAGLRAQA EQAFGENYAN AMFGLARNSV
FFPSLILIDL SFGLTLRTFY PVSASETLVT GWQIIPKGVD EEFVKYRIDN ALTFWGPAGL
ATPDDVEALE QAQKGFGARG EVGWSDVSKG MGKPVPAAND ELQMRSWWRE WNRRITGEQL
PTEGTSFVPF DKQGVDA
//
