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Database: UniProt
Entry: Q8L0Y4_9MICO
LinkDB: Q8L0Y4_9MICO
Original site: Q8L0Y4_9MICO 
ID   Q8L0Y4_9MICO            Unreviewed;       474 AA.
AC   Q8L0Y4;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Alpha subunit of dibenzofuran dioxygenase {ECO:0000313|EMBL:BAC06602.1};
GN   Name=dfdA1 {ECO:0000313|EMBL:BAC06602.1};
OS   Terrabacter sp. YK3.
OG   Plasmid pYK3 {ECO:0000313|EMBL:BAC06602.1}.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Terrabacter.
OX   NCBI_TaxID=169538 {ECO:0000313|EMBL:BAC06602.1};
RN   [1] {ECO:0000313|EMBL:BAC06602.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YK3 {ECO:0000313|EMBL:BAC06602.1};
RC   PLASMID=pYK3 {ECO:0000313|EMBL:BAC06602.1};
RX   PubMed=12147464; DOI=10.1128/AEM.68.8.3716-3723.2002;
RA   Iida T., Mukouzaka Y., Nakamura K., Kudo T.;
RT   "Plasmid-borne genes code for an angular dioxygenase involved in
RT   dibenzofuran degradation by Terrabacter sp. strain YK3.";
RL   Appl. Environ. Microbiol. 68:3716-3723(2002).
RN   [2] {ECO:0000313|EMBL:BAC06602.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YK3 {ECO:0000313|EMBL:BAC06602.1};
RC   PLASMID=pYK3 {ECO:0000313|EMBL:BAC06602.1};
RX   PubMed=18952799; DOI=10.1128/JB.01112-08;
RA   Iida T., Waki T., Nakamura K., Mukouzaka Y., Kudo T.;
RT   "The GAF-like-domain-containing transcriptional regulator DfdR is a sensor
RT   protein for dibenzofuran and several hydrophobic aromatic compounds.";
RL   J. Bacteriol. 191:123-134(2009).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR   EMBL; AB075242; BAC06602.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8L0Y4; -.
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:BAC06602.1};
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   Plasmid {ECO:0000313|EMBL:BAC06602.1}.
FT   DOMAIN          66..147
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   474 AA;  53058 MW;  89280EA322330EA3 CRC64;
     MLTVNDSGQL VSPNGQTPQA PPVNPALSSQ LKELSESEGG LLDRRMFFDP EIYKVELERV
     FARSWSFLCH ESQLAKAGDF FSTYIGADPV VVTRQRDGSI SAVLNSCRHR GMKVCRADWG
     NAKAFTCTYH GWSYSTDGSL VSVPREEYAY YNEIDKSKLG LLRVPQVQSY KGLVFGCFDP
     EAPSLVDFLG DMTYYLDILL DRVDGGTEVI SGVHKWKMRG NWKLAAEQFS GDNYHTISSH
     ISVLLSEFPP EAADAFVNID GLEINPAEGH GIGVMYSPTG APFSAGSSEA ILRWRDETRQ
     ESINRLGKER VEGMSWTHAN VFPNFSYLHD SSVLRVWMPK SPTEMEAWSW CIVDKKAPQE
     VKNAWRTQAI RHFSPGGTWE QDDGENWSYC SGAGGQEGVV TRLSKLHVEM GVGHERSHPT
     LPGKVSHTYS EQNQRSLYRR WAEFMAAESW KDISVPVRTT EVIDRSDMAK AGES
//
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