ID A0A1R4FAB6_9ACTO Unreviewed; 443 AA.
AC A0A1R4FAB6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Ring hydroxylating dioxygenase alpha subunit {ECO:0000313|EMBL:SJM52854.1};
GN ORFNames=CZ771_05925 {ECO:0000313|EMBL:SJM52854.1};
OS Actinomycetales bacterium JB111.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales.
OX NCBI_TaxID=1434822 {ECO:0000313|EMBL:SJM52854.1, ECO:0000313|Proteomes:UP000196124};
RN [1] {ECO:0000313|EMBL:SJM52854.1, ECO:0000313|Proteomes:UP000196124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB111 {ECO:0000313|EMBL:SJM52854.1,
RC ECO:0000313|Proteomes:UP000196124};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; FUHX01000026; SJM52854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4FAB6; -.
DR OrthoDB; 5243643at2; -.
DR Proteomes; UP000196124; 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 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:SJM52854.1};
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:UP000196124}.
FT DOMAIN 50..159
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 443 AA; 49827 MW; 423489EB5ED8DE02 CRC64;
MTAEPVGAGI EEVLEKIGEG VPEGRLPAYV YNDQRIFDLE QDRVFLKAWC FLAHETEIPK
NGDYVTRYIG NNNIIVARDE KGEIHASFNM CRHRGNMMCK SEMGNASHFR CSYHGWVYKN
SGELIGVPYM KEGYEGRLKR KDWGLLPVRT ETYAGLVFGT LDPDAEPLTD YLGDFTFYLD
FFLKQGNAGS EVHGPPDHWI TETDWKIAAE NFAGDGYHTP VAHQFGFNLG YFPSSGSTHS
QGWAASIPGK GHGIGLGHSP NFPPFAGFPD EVVASMKEAW TDEQIEVFSQ VRTGVGTVFP
NLSFLMQPFS LVPGEAGVRF TTMRLYHPIG PGKTEMYSWC LVPKDAPQEY KDEAYRCYTL
AFAQAGTFEQ DDLENWARVT RSAKSSIVRD RGVQFPYIMG MESEPDPEFA GPGHVVTPYV
NDTNFRNLWS RWSDYLTGKA WSK
//
