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Database: UniProt
Entry: G3KEB2_9BURK
LinkDB: G3KEB2_9BURK
Original site: G3KEB2_9BURK 
ID   G3KEB2_9BURK            Unreviewed;       470 AA.
AC   G3KEB2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Tert-butyl alcohol monooxygenase {ECO:0000313|EMBL:AEO00201.1};
GN   Name=mdpJ {ECO:0000313|EMBL:AEO00201.1};
OS   Methylibium sp. R8.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=394742 {ECO:0000313|EMBL:AEO00201.1};
RN   [1] {ECO:0000313|EMBL:AEO00201.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R8 {ECO:0000313|EMBL:AEO00201.1};
RX   PubMed=21742915; DOI=10.1128/AEM.00093-11;
RA   Schafer F., Muzica L., Schuster J., Treuter N., Rosell M., Harms H.,
RA   Muller R.H., Rohwerder T.;
RT   "Formation of Alkenes via Degradation of tert-Alkyl Ethers and Alcohols by
RT   Aquincola tertiaricarbonis L108 and Methylibium spp.";
RL   Appl. Environ. Microbiol. 77:5981-5987(2011).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR   EMBL; JN197272; AEO00201.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3KEB2; -.
DR   BRENDA; 1.14.13.229; 14566.
DR   BRENDA; 1.14.19.48; 14566.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044270; P:cellular nitrogen compound catabolic process; IEA:UniProt.
DR   GO; GO:1901565; P:organonitrogen compound catabolic process; IEA:UniProt.
DR   CDD; cd03479; Rieske_RO_Alpha_PhDO_like; 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   PANTHER; PTHR21266:SF60; CHOLESTEROL 7-DESATURASE; 1.
DR   PANTHER; PTHR21266; IRON-SULFUR DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF00355; Rieske; 1.
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   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Monooxygenase {ECO:0000313|EMBL:AEO00201.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          51..155
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   470 AA;  52909 MW;  1AED7AE6F2F5F3C7 CRC64;
     MGNREPLAAA GQGTAYSGYR LRDLQNAAPT NLEILRTGPG TPMGEYMRRY WQPVCLSQEL
     TDVPKAIRIL HEDLVAFRDR QGNVGVLHRK CAHRGASLEF GIVQERGIRC CYHGWHFDVD
     GKLLEAPAEP PDTKLKETVC QGAYPAFERD GLVFAYMGPA DRRPEFPVFD GYVLPKGTRL
     IPFSNVFDCN WLQVYENQID HYHTALLHNN MTVAGVDSKL ADGATLQGGF GEMPIIDWHP
     TDDNNGMIFT AGRRLSDDEV WIRISQMGLP NWMQNAAIVA AAPQRHSGPA MSRWQVPVDD
     EHSIAFGWRH FNDEVDPEHR GREEECGVDK IDFLIGQTRH RPYEERQRVP GDYEAIVSQG
     PIAVHGLEHP GRSDVGVYMC RSLLRDAVAG KAPPDPVRVK AGSTDGQTLP RYASDSRLRI
     RRRPSREADS DVIRKAAHQV FAIMKECDEL PVVQRRPHVL RRLDEIEASL
//
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