ID A0A0D5AB03_9NOCA Unreviewed; 422 AA.
AC A0A0D5AB03;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Dioxygenase hydroxylase component {ECO:0000313|EMBL:AJW40307.1};
GN ORFNames=NY08_2279 {ECO:0000313|EMBL:AJW40307.1};
OS Rhodococcus sp. B7740.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW40307.1, ECO:0000313|Proteomes:UP000032410};
RN [1] {ECO:0000313|EMBL:AJW40307.1, ECO:0000313|Proteomes:UP000032410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7740 {ECO:0000313|EMBL:AJW40307.1};
RX PubMed=25931596;
RA Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.;
RT "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid-Producing
RT Bacterium Isolated from the Arctic Sea.";
RL Genome Announc. 3:0-0(2015).
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; CP010797; AJW40307.1; -; Genomic_DNA.
DR RefSeq; WP_045196348.1; NZ_CP010797.1.
DR AlphaFoldDB; A0A0D5AB03; -.
DR STRING; 1564114.NY08_2279; -.
DR KEGG; rhb:NY08_2279; -.
DR PATRIC; fig|1564114.4.peg.2240; -.
DR HOGENOM; CLU_026244_4_0_11; -.
DR Proteomes; UP000032410; 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:AJW40307.1};
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 37..120
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 422 AA; 47356 MW; B514C41B5DAE47C5 CRC64;
MTVDYEHLIE PDRVHGSLYT DPAIFAEEMT RIFATTWVCL GHDSEIPQPG DYIRRHLGRD
EVVVTRAKDG EIHVLLNRCA HRANLVCEDD QGNSNSFRCP YHGWTYGNDG ELLGYPYFKG
YGGKGKLDLR LGSAARVDTY QGFIFASMAA EGPTLIEHLG PAAGEMDRLA ALSPTGEIEL
TGTWMKHRAR ANWKMLVENE TDGYHPQFVH GSIISVSGHA LGHLYSEKSK SVVRALGNGH
SELDQREEFR HIDKPLMWFD TTPERLPDYV AQMREKHGED TDRLLIDGAP HVMVYPNLFI
AEVTIFLIEP VGVDETIQHS TPVQFKGSPD INRRLISQSM ASVGPAGMLL ADDTEMYERN
QAGVQASQPE WLVLKRGLDR EWVDDDGLQV GVGNDETAMR AFWSHYRTVM TDDEPSTSEV
SQ
//
