MDPJ_AQUTE
ID MDPJ_AQUTE Reviewed; 470 AA.
AC G8FRC5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Tert-butanol monooxygenase / tert-amyl alcohol desaturase oxygenase subunit {ECO:0000305};
DE EC=1.14.13.229 {ECO:0000269|PubMed:22194447};
DE EC=1.14.19.48 {ECO:0000269|PubMed:22194447};
DE AltName: Full=Rieske nonheme mononuclear iron oxygenase MdpJ {ECO:0000303|PubMed:22194447};
GN Name=mdpJ {ECO:0000303|Ref.1};
OS Aquincola tertiaricarbonis.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Aquincola.
OX NCBI_TaxID=391953;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=L108;
RA Schaefer F., Breuer U., Benndorf D., von Bergen M., Harms H., Mueller R.H.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=L108;
RX PubMed=22194447; DOI=10.1128/jb.06384-11;
RA Schuster J., Schaefer F., Huebler N., Brandt A., Rosell M., Haertig C.,
RA Harms H., Mueller R.H., Rohwerder T.;
RT "Bacterial degradation of tert-amyl alcohol proceeds via hemiterpene 2-
RT methyl-3-buten-2-ol by employing the tertiary alcohol desaturase function
RT of the Rieske nonheme mononuclear iron oxygenase MdpJ.";
RL J. Bacteriol. 194:972-981(2012).
RN [3]
RP INDUCTION.
RC STRAIN=L108;
RX DOI=10.1002/elsc.200700011;
RA Schaefer F., Breuer U., Benndorf D., von Bergen M., Harms H., Mueller R.H.;
RT "Growth of Aquincola tertiaricarbonis L108 on tert-butyl alcohol leads to
RT the induction of a phthalate dioxygenase-related protein and its associated
RT oxidoreductase subunit.";
RL Eng. Life Sci. 7:512-519(2007).
RN [4]
RP FUNCTION, AND BIOTECHNOLOGY.
RC STRAIN=L108;
RX PubMed=22752178; DOI=10.1128/aem.01434-12;
RA Schaefer F., Schuster J., Wuerz B., Haertig C., Harms H., Mueller R.H.,
RA Rohwerder T.;
RT "Synthesis of short-chain diols and unsaturated alcohols from secondary
RT alcohol substrates by the Rieske nonheme mononuclear iron oxygenase MdpJ.";
RL Appl. Environ. Microbiol. 78:6280-6284(2012).
CC -!- FUNCTION: Oxygenase component of a two-component system involved in the
CC degradation of tertiary alcohols such as tert-butyl alcohol (TBA) and
CC tert-amyl alcohol (TAA). In the presence of TBA, catalyzes the
CC hydroxylation of TBA to 2-methylpropane-1,2-diol. In the presence of
CC TAA, functions as a desaturase, enabling the degradation of TAA and
CC resulting in the formation of the hemiterpene 3-hydroxy-3-methylbut-1-
CC ene. The specificity of the catalysis depends strongly on the molecule
CC structure of the substrate, allowing either hydroxylation or
CC desaturation reactions (PubMed:22194447). Also catalyzes the
CC desaturation of the tertiary alcohol 3-methyl-3-pentanol (a C6 homolog
CC of TBA and TAA) to 3-methyl-1-penten-3-ol, with lower efficiency
CC (PubMed:22194447). In addition, can transform some secondary alcohols,
CC including the hydroxylation of 2-propanol to 1,2-propanediol, and the
CC desaturation of 2-butanol, 3-methyl-2-butanol and 3-pentanol
CC (PubMed:22752178). {ECO:0000269|PubMed:22194447,
CC ECO:0000269|PubMed:22752178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + tert-butanol = 2-methylpropane-1,2-diol +
CC H2O + NADP(+); Xref=Rhea:RHEA:50012, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:45895,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:131845;
CC EC=1.14.13.229; Evidence={ECO:0000269|PubMed:22194447};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50013;
CC Evidence={ECO:0000269|PubMed:22194447};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylbutan-2-ol + H(+) + NADPH + O2 = 3-hydroxy-3-
CC methylbut-1-ene + 2 H2O + NADP(+); Xref=Rhea:RHEA:50368,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132750,
CC ChEBI:CHEBI:132752; EC=1.14.19.48;
CC Evidence={ECO:0000269|PubMed:22194447};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50369;
CC Evidence={ECO:0000269|PubMed:22194447};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- SUBUNIT: This two-component enzyme is composed of an oxygenase (MdpJ)
CC and a reductase (MdpK). {ECO:0000269|PubMed:22194447}.
CC -!- INDUCTION: Induced in the presence of tert-butyl alcohol (TBA).
CC {ECO:0000269|Ref.3}.
CC -!- DISRUPTION PHENOTYPE: Mutants are not able to grow on the tertiary
CC alcohols TBA and TAA. {ECO:0000269|PubMed:22194447}.
CC -!- BIOTECHNOLOGY: Shows a biotechnological potential for the synthesis of
CC enantiopure short-chain diols and unsaturated alcohols from secondary
CC alcoholic precursors. {ECO:0000269|PubMed:22752178}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000305}.
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DR EMBL; JN033363; AER12131.1; -; Genomic_DNA.
DR EMBL; JQ062962; AEX20406.1; -; Genomic_DNA.
DR KEGG; ag:AEX20406; -.
DR BRENDA; 1.14.13.229; 14508.
DR BRENDA; 1.14.19.48; 14508.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding; Monooxygenase; NADP;
KW Oxidoreductase.
FT CHAIN 1..470
FT /note="Tert-butanol monooxygenase / tert-amyl alcohol
FT desaturase oxygenase subunit"
FT /id="PRO_0000455120"
FT DOMAIN 51..155
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 91
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 93
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 110
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 113
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 470 AA; 52866 MW; 44F8CD2BEDC2C1A0 CRC64;
MGNREPLAAA GQGTAYSGYR LRDLQNVAPT NLEILRTGPG TPMGEYMRRY WQPVCLSQEL
TDVPKAIRIL HEDLVAFRDR RGNVGVLHRK CAHRGASLEF GIVQERGIRC CYHGWHFDVD
GSLLEAPAEP PDTKLKETVC QGAYPAFERN GLVFAYMGPA DRRPEFPVFD GYVLPKGTRL
IPFSNVFDCN WLQVYENQID HYHTALLHNN MTVAGVDAKL ADGATLQGGF GEMPIIDWHP
TDDNNGMIFT AGRRLSDDEV WIRISQMGLP NWMQNAAIVA AAPQRHSGPA MSRWQVPVDD
EHSIAFGWRH FNDEVDPEHR GREEECGVDK IDFLIGQTRH RPYEETQRVP GDYEAIVSQG
PIALHGLEHP GRSDVGVYMC RSLLRDAVAG KAPPDPVRVK AGSTDGQTLP RYASDSRLRI
RRRPSREADS DVIRKAAHQV FAIMKECDEL PVVQRRPHVL RRLDEIEASL
