ID G8RMP7_MYCRN Unreviewed; 460 AA.
AC G8RMP7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Ring-hydroxylating dioxygenase, large terminal subunit {ECO:0000313|EMBL:AEV73714.1};
GN OrderedLocusNames=MycrhN_3181 {ECO:0000313|EMBL:AEV73714.1};
OS Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV73714.1, ECO:0000313|Proteomes:UP000005442};
RN [1] {ECO:0000313|EMBL:AEV73714.1, ECO:0000313|Proteomes:UP000005442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB3 {ECO:0000313|EMBL:AEV73714.1,
RC ECO:0000313|Proteomes:UP000005442};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL Submitted (DEC-2011) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003169; AEV73714.1; -; Genomic_DNA.
DR RefSeq; WP_014211473.1; NC_016604.1.
DR AlphaFoldDB; G8RMP7; -.
DR STRING; 710685.MycrhN_3181; -.
DR KEGG; mrh:MycrhN_3181; -.
DR PATRIC; fig|710685.3.peg.3188; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_026244_4_0_11; -.
DR OrthoDB; 5243643at2; -.
DR Proteomes; UP000005442; 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 GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08881; RHO_alpha_C_NDO-like; 1.
DR CDD; cd03535; Rieske_RO_Alpha_NDO; 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; IPR043257; Rieske_N.
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:AEV73714.1};
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:UP000005442}.
FT DOMAIN 62..146
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 460 AA; 51104 MW; AECDAB3EE1C3F91B CRC64;
MFLQAGIDRK VRLVNSMAPD ATTMRLLENA RGSILKGRLP ASLIANAALY QLELKRVFGR
TWQFLCHEDE IPNPGDYVVR YIADNSIIVA RQQDMTIRAM SNSCRHRGTL LCRTEAGNES
AFQCPYHGWT YRNNGDLIAI PAQQAVYGAA FDKSRLGLRA LPMLDSYAGL VFGCVSDEAP
GLDEYLGDMR WYLDLMMSKS AAGIQVWGAP QRWVIDANWK TGADNFVGDG YHTVMTHRSM
CELGLLPPDN VAVSPAHVSL SGGHGAGVLG APPGIPAPPY MGYPEEIVSG LSEGYGDDVH
GEMLKRTMFI HGNVFPNLSF LNAFIAKDGE SMPVPILTLR QWRPLDAARM EVWSWFFVER
NAPEEFKQQS FETYVRTFGV GGVFEQDDAE IFQAITKGTR GELAGGVELN VEMGLDNLAP
DPTWLGPGRP LASGYAEQNQ REYWKQYFDY LATPRRDENV
//
