MDPK_AQUTE
ID MDPK_AQUTE Reviewed; 337 AA.
AC G8FRC6;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Tert-butanol monooxygenase / tert-amyl alcohol desaturase reductase subunit {ECO:0000305};
DE EC=1.-.-.- {ECO:0000305};
GN Name=mdpK {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, AND SUBUNIT.
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.
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: Reductase 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) (PubMed:22194447). MdpK probably provides
CC electrons via its [2Fe-2S] iron-sulfur cluster to the MdpJ oxygenase
CC subunit (Probable). {ECO:0000269|PubMed:22194447,
CC ECO:0000305|PubMed:22752178}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00465};
CC Note=Binds 1 2Fe-2S cluster. {ECO:0000255|PROSITE-ProRule:PRU00465};
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 -!- SIMILARITY: Belongs to the PDR/VanB family. {ECO:0000305}.
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DR EMBL; JN033364; AER12132.1; -; Genomic_DNA.
DR EMBL; JQ062962; AEX20407.1; -; Genomic_DNA.
DR KEGG; ag:AEX20407; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR000951; Ph_dOase_redase.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Electron transport; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Transport.
FT CHAIN 1..337
FT /note="Tert-butanol monooxygenase / tert-amyl alcohol
FT desaturase reductase subunit"
FT /id="PRO_0000455121"
FT DOMAIN 9..114
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT DOMAIN 254..337
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 288
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 293
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 296
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 324
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 337 AA; 36966 MW; 1E37730395A0F0C1 CRC64;
MYQLSHTGKY PKTALNLRVR QITYQGIGIN AYEFVREDGG ELEEFTAGAH VDLYFRDGRV
RQYSLCNDPA ERRRYLIAVL RDDNGRGGSI AIHERVHTQR LVAVGHPRNN FPLIEGAPHQ
VLLAGGIGIT PLKAMVHRLE RMGADYTLHY CAKSSAHAAF QEELAPMAAK GRVIMHFDGG
NPAKGLDIAA LLRRYEPGWQ LYYCGPPGFM EACTRACTHW PAEAVHFEYF VGAPVLPDDG
VPQDIGSDAL ALGFQIKIAS TGTVLTVPND KSIAQVLGEH GIEVPTSCQS GLCGTCKVRY
LAGDVEHRDY LLSAEARTQF LTTCVSRSKG ATLVLDL
